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Human Metabolome Database Version 2.5

 

Showing metabocard for Palmitic acid (HMDB00220)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-11-16 11:38:08
Accession Number HMDB00220
Secondary Accession Numbers Not Available
Common Name Palmitic acid
Description Palmitic acid, or hexadecanoic acid is one of the most common saturated fatty acids found in animals and plants, a saturated fatty acid found in fats and waxes including olive oil, palm oil, and body lipids.(wikipedia) Biological Source: Occurs in the form of esters (glycerides) in oils and fats of vegetable and animal origin. Usually obtained from palm oil. Widely distributed in plants Use/Importance: Used in determination of water hardness Biological Use/Importance: Active ingredient of *Levovist*TM, used in echo enhancement in sonographic Doppler B-mode imaging. Ultrasound contrast medium (Dictionary of Organic Compounds)
Synonyms
  1. Hexaectylic acid
  2. Lunac P 95KC
  3. Prifac 2960
  4. Palmitate
  5. Hydrofol
  6. PLM
  7. Lunac P 95
  8. Hexadecylic acid
  9. Hystrene 8016
  10. Industrene 4516
  11. Hexadecoic acid
  12. Lunac P 98
  13. Emersol 140
  14. Hexadecanoic acid
  15. PAM
  16. Kortacid 1698
  17. Hydrofol acid 1690
  18. Pristerene 4934
  19. Prifrac 2960
  20. Univol U332
  21. 1-hexyldecanoic acid
  22. palmitic acid
  23. Palmitinsaeure
  24. C16 fatty acid
  25. Loxiol EP 278
  26. Emersol 143
  27. Edenor C16
  28. Hystrene 9016
  29. 1-Pentadecanecarboxylic acid
  30. Cetylic acid
  31. Glycon P-45
  32. Hexadecanoate
  33. Palmitinate
  34. Palmitinic acid
  35. Pentadecanecarboxylate
  36. Pentadecanecarboxylic acid
  37. n-Hexadecanoate
  38. n-Hexadecanoic acid
  39. n-Hexadecoate
  40. n-Hexadecoic acid
  41. Hexadecanoic acid palmitic acid
  42. Hexadecoate
  43. 1-hexyldecanoate
  44. palmitoate
  45. palmitoic acid
Chemical IUPAC Name Hexadecanoic acid
Chemical Formula C16H32O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Fatty Acids
Sub Class
  • Long chain fatty acids
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 256.424
Monoisotopic Molecular Weight 256.240234
Isomeric SMILES CCCCCCCCCCCCCCCC(O)=O
Canonical SMILES CCCCCCCCCCCCCCCC(O)=O
KEGG Compound ID C00249 Link Image
BioCyc ID CPD-8475 Link Image
BiGG ID 34386 Link Image
Wikipedia Link Palmitic acid Link Image
NuGOwiki Link HMDB00220 Link Image
Metagene Link HMDB00220 Link Image
METLIN ID 187 Link Image
PubChem Compound 985 Link Image
PubChem Substance 841623 Link Image
ChEBI ID 15756 Link Image
CAS Registry Number 57-10-3
InChI Identifier InChI=1/C16H32O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16(17)18/h2-15H2,1H3,(H,17,18)
Synthesis Reference Xu, Yan; Ling, Li. A method for preparing conjugated linoleic acid and palmitic acid. Faming Zhuanli Shenqing Gongkai Shuomingshu (2005), 5 pp.
Melting Point (Experimental) 61.8 oC
Experimental Water Solubility 4e-05 mg/mL [ROBB.ID (1966)] Source: PhysProp
Predicted Water Solubility 4.07e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity 7.17 [SANGSTER (1993)] Source: PhysProp
Predicted LogP/Hydrophobicity 7.23 [Predicted by ALOGPS]; 6.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1B0O Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • endoplasmic reticulum
  • Extracellular
  • peroxisome
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Adipose Tissue
Bladder
Epidermis
Fibroblasts
Kidney
Platelet
Skeletal Muscle
Stratum Corneum
Concentrations (Normal)
Biofluid Blood
Value 25.0 +/- 2.8 uM
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 25.5 +/- 2.8 uM
Age Adolescent:13-18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 26.7 +/- 4.4 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 30.49 +/- 2.64 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Min Y, Ghebremeskel K, Lowy C, Thomas B, Crawford MA: Adverse effect of obesity on red cell membrane arachidonic and docosahexaenoic acids in gestational diabetes. Diabetologia. 2004 Jan;47(1):75-81. Epub 2003 Nov 22. [PubMed Link Image]
Biofluid Blood
Value 66.010 +/- 9.879 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Nikolaos Psychogios, David D. Hau, Jun Peng, An Chi Guo, Rupasri Mandal, Souhaila Bouatra, Igor Sinelnikov, Ramanarayan Krishnamurthy, Roman Eisner, Bijaya Gautam, Nelson Young, Jinaguo Xia, Craig Knox, Ying Wei Dong, Paul Huang, Janet McManus, Theresa Pedersen, Fiona Bamforth, Russ Greiner, Bruce McManus, John Newman, David S. Wishart, The Human Serum Metabolome, PLoS ONE (Submitted).
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
Biofluid CSF
Value 18.0 +/- 12.0 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
Biofluid Urine
Value 11.2 (6.0-26.1) umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 2.2 (0.8-8.2) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Children aged 2-6 years
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 1.4 (0.1-3.8) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Children aged 6-10 years
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 10.8 (2.6-32.7) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 1.4 (0.1-7.3) umol/mmol creatinine
Age Adolescent:13-18 yrs old
Sex Both
Patient information Normal
Comments Children >10 years old
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 0.30 +/- 0.09 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Fatty Acid Biosynthesis SMP00456 Link Image
Fatty Acid Elongation In Mitochondria SMP00054 Link Image map00062 Link Image
Fatty acid Metabolism SMP00051 Link Image map00071 Link Image
Glycerolipid Metabolism SMP00039 Link Image map00561 Link Image
General References
  1. Lloyd B, Halter RJ, Kuchan MJ, Baggs GE, Ryan AS, Masor ML: Formula tolerance in postbreastfed and exclusively formula-fed infants. Pediatrics. 1999 Jan;103(1):E7. [PubMed Link Image]
  2. Katsuta Y, Iida T, Inomata S, Denda M: Unsaturated fatty acids induce calcium influx into keratinocytes and cause abnormal differentiation of epidermis. J Invest Dermatol. 2005 May;124(5):1008-13. [PubMed Link Image]
  3. Mensink RP: Nutrition in lipid disorders. Ther Umsch. 1995 Aug;52(8):509-14. [PubMed Link Image]
  4. Mesiha MS, Ponnapula S, Plakogiannis F: Oral absorption of insulin encapsulated in artificial chyles of bile salts, palmitic acid and alpha-tocopherol dispersions. Int J Pharm. 2002 Dec 5;249(1-2):1-5. [PubMed Link Image]
  5. Dubinin DM, Naidina VP, Zaloguev SN: [Evaluation of human skin function in a sealed room by a chromatographic method] Kosm Biol Aviakosm Med. 1985 Nov-Dec;19(6):69-73. [PubMed Link Image]
  6. Okun JG, Kolker S, Schulze A, Kohlmuller D, Olgemoller K, Lindner M, Hoffmann GF, Wanders RJ, Mayatepek E: A method for quantitative acylcarnitine profiling in human skin fibroblasts using unlabelled palmitic acid: diagnosis of fatty acid oxidation disorders and differentiation between biochemical phenotypes of MCAD deficiency. Biochim Biophys Acta. 2002 Oct 10;1584(2-3):91-8. [PubMed Link Image]
  7. Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
  8. Otsuki T, Oku M: [A study on the effect of cortisol and progesterone on cytosolic arachidonic and palmitic acid concentrations in cultured human myometrial cells] Nippon Sanka Fujinka Gakkai Zasshi. 1995 Jun;47(6):531-8. [PubMed Link Image]
  9. Draisey TF, Gagneja GL, Thibert RJ: Pulmonary surfactant and amniotic fluid insulin. Obstet Gynecol. 1977 Aug;50(2):197-9. [PubMed Link Image]
  10. Florentin E, Athias A, Lagrost L: Modulation of the activity of the human cholesteryl ester transfer protein by carboxylated derivatives. Evidence for 13-cis-retinoic acid as a potent activator of the protein's activity in plasma. Eur J Biochem. 1996 Sep 15;240(3):699-706. [PubMed Link Image]
  11. Urien S, Morin D, Tillement JP: Effect of alpha-1-acid glycoprotein, albumin and palmitic acid on the brain and salivary gland extraction of warfarin in rats. J Pharmacol Exp Ther. 1989 Feb;248(2):781-5. [PubMed Link Image]
  12. Wang J, Zhu F, Pan G: [Diagnosis of chylous ascites with oral administration of 13C-palmitic acid] Zhonghua Nei Ke Za Zhi. 1996 Jun;35(6):382-4. [PubMed Link Image]
  13. Ip MP, Draisey TF, Thibert RJ, Gagneja GL, Jasey GM: Fetal lung maturity, as assessed by gas-liquid chromatographic determination of phospholipid palmitic acid in amniotic fluid. Clin Chem. 1977 Jan;23(1):35-40. [PubMed Link Image]
  14. Messner T, Erkstam UB, Gustafsson IB, Nilsson SB, Vessby B: Diet and dietary markers in Kiruna and Uppsala, Sweden--a comparison. Int J Circumpolar Health. 1997 Apr;56(1-2):21-9. [PubMed Link Image]
  15. A J, Trygg J, Gullberg J, Johansson AI, Jonsson P, Antti H, Marklund SL, Moritz T: Extraction and GC/MS analysis of the human blood plasma metabolome. Anal Chem. 2005 Dec 15;77(24):8086-94. [PubMed Link Image]
  16. Vessby B, Tengblad S, Lithell H: Insulin sensitivity is related to the fatty acid composition of serum lipids and skeletal muscle phospholipids in 70-year-old men. Diabetologia. 1994 Oct;37(10):1044-50. [PubMed Link Image]
  17. Liau YH, Slomiany BL, Slomiany A, Piasek A, Palmer D, Rosenthal WS: Identification of mucus glycoprotein fatty acyltransferase activity in human gastric mucosa. Digestion. 1985;32(1):57-62. [PubMed Link Image]
  18. Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
  19. Cater NB, Denke MA: Behenic acid is a cholesterol-raising saturated fatty acid in humans. Am J Clin Nutr. 2001 Jan;73(1):41-4. [PubMed Link Image]
  20. Wikipedia Link Image
Metabolic Enzymes
  1. Fatty acid synthase
  2. Calcium-dependent phospholipase A2 precursor
  3. Group IIF secretory phospholipase A2 precursor
  4. Cytosolic phospholipase A2
  5. Phospholipase A2 precursor
  6. Group 10 secretory phospholipase A2 precursor
  7. Galactoside-binding soluble lectin 13
  8. Group IIE secretory phospholipase A2 precursor
  9. Group XIIA secretory phospholipase A2 precursor
  10. 85 kDa calcium-independent phospholipase A2
  11. Eosinophil lysophospholipase
  12. Phospholipase A2, membrane associated precursor
  13. Group IID secretory phospholipase A2 precursor
  14. Pancreatic triacylglycerol lipase precursor
  15. Hepatic triacylglycerol lipase precursor
  16. Pancreatic lipase-related protein 1 precursor
  17. Adiponutrin
  18. Gastric triacylglycerol lipase precursor
  19. Endothelial lipase precursor
  20. Bile salt-activated lipase precursor
  21. Pancreatic lipase-related protein 2 precursor
  22. Lipoprotein lipase precursor
  23. Liver carboxylesterase 1 precursor
  24. Carboxylesterase 2 precursor
  25. Cholinesterase precursor
  26. Cytosolic phospholipase A2 gamma precursor
  27. Hormone-sensitive lipase
  28. Group 3 secretory phospholipase A2 precursor
  29. Bile acid CoA:amino acid N-acyltransferase
  30. Acylphosphatase-2
  31. Acylphosphatase-1
  32. Aminoacylase-1
  33. Aspartoacylase
  34. Aspartoacylase-2
  35. Long-chain-fatty-acid--CoA ligase 4
  36. Long-chain-fatty-acid--CoA ligase 1
  37. Long-chain-fatty-acid--CoA ligase 6
  38. Long-chain-fatty-acid--CoA ligase 5
  39. Long-chain-fatty-acid--CoA ligase 3
  40. Cytosolic acyl coenzyme A thioester hydrolase
  41. Acyl-coenzyme A thioesterase 2
  42. Acyl-coenzyme A thioesterase 8
  43. Palmitoyl-protein thioesterase 1 precursor
  44. Acid ceramidase precursor
  45. Peroxisome proliferator-activated receptor gamma
  46. Long-chain fatty acid transport protein 6
  47. Thioesterase domain containing 1
  48. Long-chain fatty acid transport protein 3
  49. Patatin-like phospholipase domain-containing protein 4
  50. Long-chain fatty acid transport protein 1
  51. Long-chain fatty acid transport protein 4
  52. Full-length cDNA clone CS0DM001YM08 of Fetal liver of Homo sapiens
  53. Phospholipase B1
  54. Patatin-like phospholipase domain-containing protein 2
  55. Cytosolic phospholipase A2 delta
  56. Cytosolic phospholipase A2 epsilon
  57. Cytosolic phospholipase A2 zeta
  58. Calcium-independent phospholipase A2-gamma
  59. Cytosolic phospholipase A2 beta
  60. Putative neutral ceramidase C
  61. Alkaline ceramidase 2
  62. Alkaline ceramidase 2
  63. Neutral ceramidase
  64. Acyl-CoA thioesterase 4
  65. Carboxylesterase 7
  66. Palmitoyl-protein thioesterase 2 (HCG1999928, isoform CRA_a)
  67. Alkaline ceramidase 1
  68. Neuropathy target esterase
  69. Pancreatic lipase-related protein 3
  70. Carnitine palmitoyltransferase 1B isoform a variant
  71. cDNA FLJ76296, highly similar to Homo sapiens carnitine palmitoyltransferase 1B (muscle) (CPT1B), transcript variant 1, mRNA
  72. Carboxylesterase 3
  73. Peroxisome proliferative acitvated receptor gamma
  74. CREB3L2-PPARgamma
  75. cDNA FLJ57380, highly similar to Adipophilin
  76. Adipose differentiation-related protein
  77. ADFP protein
  78. Peroxisome proliferator activated-receptor gamma
  79. cDNA FLJ53798, highly similar to Long-chain fatty acid transport protein 1 (EC 6.2.1.-)
  80. Peroxisome proliferative activated receptor gamma isoform 2 variant
  81. cDNA FLJ14598 fis, clone NT2RM4002558, highly similar to Long-chain fatty acid transport protein 4 (EC 6.2.1.-)
  82. cDNA FLJ61377, highly similar to Long-chain fatty acid transport protein 1 (EC 6.2.1.-)
  83. CPT1B protein
  84. Peroxisome proliferator-activated receptor gamma 1
  85. CPT1B protein
  86. cDNA FLJ90350 fis, clone NT2RP2003210, highly similar to Long-chain fatty acid transport protein 4 (EC 6.2.1.-)
  87. cDNA FLJ50069, highly similar to Long-chain fatty acid transport protein 1 (EC 6.2.1.-)
Enzyme 1 [top]
Enzyme 1 ID 5264
Enzyme 1 Name Fatty acid synthase
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name FASN
Enzyme 1 Protein Sequence >Fatty acid synthase
MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRF
DASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL
SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQC
PAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR
RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVG
DPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH
SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATL
PRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP
EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLS
TDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV
LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFE
FVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA
QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCT
IIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL
AWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLA
RALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQ
WDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRL
LWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVV
SRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQL
CKGLVQALQTTVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQ
VLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLL
SPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVA
ALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESL
FSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRP
VWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGD
LVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPG
AQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAK
GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGV
GQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKG
VDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFF
NESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEE
PEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGI
RTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL
ENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSA
MERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLN
QPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSV
EVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLR
SLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLD
SIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGS
PTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAA
VDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGA
DYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG
Enzyme 1 Number of Residues 2511
Enzyme 1 Molecular Weight 273403
Enzyme 1 Theoretical pI 6.39
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • oxidoreductase activity
  • phosphopantetheine binding
  • transferase activity
  • vitamin binding
Process
  • biosynthesis
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid biosynthesis
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
Enzyme 1 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 1 Specific Function Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (3R)-3-hydroxypalmitoyl-[acyl-carrier protein] = 2-hexadecenoyl-[acyl-carrier protein] + H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1049053 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P49327 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name FAS_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >7515 bp
ATGGAGGAGGTGGTGATTGCCGGCATGTTCGGGAAGCTGCCAGAGTCGGAGAACTTGCAG
GAGTTCTGGGACAACCTCATCGGCGGTGTGGACATGGTCACGGACGATGACCGTCGCTGG
AAGGCTGGGCTCTACGGCCTGCCCCGGCGGTCCGGCAAGCTGAAGGACCTGTCTAGGTTT
GATGCCTCCTTCTTCGGAGTCCACCCCAAGCAGGCACACACGATGGACCCTCAGCTGCGG
CTGCTGCTGGAAGCTACCTATGAAGCCATCGTGGACGGAGGCATCAACCCAGATTCACTC
CGAGGAACACACACTGGCGTCTGGGTGGGCGTGAGCGGCTCTGAGACCTCGGAGGCCCTG
AGCCGAGACCCCGAGACACTCGTGGGCTACAGCATGGTGGGCTGCCAGCGAGCGATGATG
GCCAACCGGCTCTCCTTCTTCTTCGACTTCAGAGGGCCCAGCATCGCACTGGACACAGCC
TGCTCCTCCAGCCTGATGGCCCTGCAGAACGCCTACCAGGCCATCCACAGCGGGCAGTGC
CCTGCCGCCATCGTGGGGGGCATCAACGTCCTGCTGAAGCCCAACACCTCCGTGCAGTTC
TTGAGGCTGGGGATGCTCAGCCCCGAGGGCACCTGCAAGGCCTTCGACACAGCGGGGAAT
GGGTACTGCCGCTCGGAGGGTGTGGTGGCTGTCCTGCTGACCAAGAAGTCCCTGGCCCGG
AAGGTCTACACCACCATCCTGAACAAAGGCACCAATACAGATGGCTTCAAGGAGCAAGGC
GTGACCTTCCCTCAGGATATCCAGGAGCAGCCTATCCGCTCGTTGTACCAGTCGGCCGGA
GTGGCCCCTGAGTCATTTGAATACATCGAAGCCCACGGACCAGGCACCAAGGTGGGCGAC
CCCCAGGAGCGTAATGGCATCACCCGAGCCCTGTGCGCCACCCGCCAGGAGCCGCTGCTC
ATCGGCTCCACCAAGTCCAACATGGGGCACCCGGAGCCAGCCTCGGGGCTCGACGCCCTG
GCCAAGGTGCTGCTGTCCCTGGAGCACGGGCTCTGGGCCCCCAACCTGCACTTCCATAGC
CCCAACCCTGAGATCCCAGCGCTGTTGGATGGGCGGCTGCAGGTGGTGGACCAGCCCCTG
CCCGTCCGTGGCGGCAACGTGGGCATCAACTCCTTTGGCTTCGGGGGCTCCAACATGCAC
ATCATCCTGAGGCCCAACACGCAGTCCGCCCCCGCACCCGCCCCACATGCCACCCTGCCC
CGTCTGCTGCGGGCCAGCGGACGCACCCCTGAGGCCGTGCAGAAGCTGCTGGAGCAGGGC
CTCCGGCACAGCCAGGGCCTGGCTTTCCTGAGCATGCTGAACGACATCGCGGCTGTCCCC
GCCACCGCCATGCCCTTCCGTGGCTACGCTGTGCTGGGTGGTGAGACGCGGTGGCCCAGA
GTGCAGCAGGTGCCCGCTGGCGAGCGCCCGCTCTGGTTCATCTGCTCTGGGATGGGCACA
CAGTGGCGTGGAATGGGGCTGAGCCTTATGCGCCTGGACCGCTTCCGAGATTCCATCCTA
CGCTCCGATGAGGCTGTGAACCGATTCGGCCTGAAGGTGTCACAGCTGCTGCTGAGCACA
GACGAGAGCACCTTTGATGACATCGTCCATTCGTTTGTGAGCCTGACTGCCATCCAGATA
GGCCTCATAGACCTGCTGAGCTGCATGGGACCTGAGGCAGATGGCATCGTCGGCCACTCC
CTGGGGGAGTGGCTGTCGGTACGCGACGGCTGCCTGTCCCAGGAGGAGGCCGTCCTCGCT
GCCTACTGGAGGGGACAGTGCATCAAAGAAGCCCCACTTCCCGCCGGCGCCATGGCAGCC
GTGGGCTTGTCCTGGGAGGAGTGTAAACAGCGCTGCCCCCCTGCGGTGGTGCCCGCCTGC
CACAACTCCAAGGACACAGTCACCATCTCGGGACCTCAGGCCCCGGTGTTTGAGTTCGTG
GAGCAGCTGAGGAAGGAGGGTGTGTTTGCCAAGGAGGTGCGGACCGGCGGTATGGCCTTC
CACTCCTACTTCATGGAGGCCATCGCACCCCCACTGCTGCAGGAGCTCAAGAAGGTGATC
CGGGAGCCGAAGCCACGTTCAGCCCGCTGGCTCAGCACCTCTATCCCCGAGGCCCAGTGG
CACAGCAGCCTGGCACGCACGTCTTCCGCCGAGTACAATGTCAACAACCTGGTGAGCCCT
GTGCTGTTCCAGGAGGCCCTGTGGCACGTGCCTGAGCACGCGGTGGTGCTGGAGATCGCC
CCGACCCCGTGCCCTCAGGCTGTCCTGAAGCGGGTCCGTAAGCCGAGCTGCACCATCATC
CCCCGTATGAAGAAGGATCACAGGGACAACCTGGAGTTCTTCCTGGCCGGCATCGGCAGG
CTGCACCTCTCAGGCATCGACGCCAACCCCAATGCCTTGTTCCCACCTGTGGAGTCCCCA
GCTCCCCGAGGAACTCCCCTCATCTCCCCACTCATCAAGTGGGACCACAGCCTGGCCTGG
GACGCGCCGGCCGCCGAGGACTTCCCCAACGGTTCAGGTTCCCCCTCAGCCACCATCTAC
ACATGCACACCAAGCTCCGAGTCTCCTGACCGCTACCTGGTGGACCACACCATCGACGGT
CGCGTCCTCTTCCCCGCCACTGGCTACCTGAGCATAGTGTGGAAGACGCTGGCCCGCGCC
TGGGCTGGGCTCGAGCAGCTGCCTGTGGTGTTTGAGGATGTGGTGCAGCACCAGGCCACC
ATCCTGCCCAAGACTGGGACAGTGTCCTTGGAGGTACGGCTCCTGGAGGCCACCGGTGCC
TTCGAGGTGTCAGAGAACGGCAACCTGGTAGTGAGTGGGAAGGTGTACCAGTGGGATGAC
CCTGACCCCAGGCTCTTCGACCACCCGGAAAGTCCCCACCCCAATTCCCCACGGAGTCCC
CTCTTCCTGGCCCAGGCAGAAGTTTACAAGGAGCTGCGTCTGCGTGGCTACGACTACGGC
CCTCATTTCCAGGGCATCCTGGAGGCCAGCCTGGAAGGTGACTCGGGGAGGCTGCTGTGG
AAGGATAACTGGGTGAGCTTCATGGACACCATGCTGCAGATGTCCATCCTGGGCTCGGCC
AAGCACGGCCTGTACCTACCCACCCGTGTCACCGCCATCCACATCGACCCTGCCACCCAC
AGGCAGAAGCTGTACACACTGCAGGACAAGGCCCAAGTGGCTGACGTGGTGGTGAGCAGG
TGGCCGAGGGTCACAGTGGCGGGAGGCGTCCACATCTCCGGGCTCCACACTGAGTCGGCC
CCGCGGCGGCACGAGGAGCAGCAGGTGCCCATCCTGGAGAAGTTTTGCTTCACTCCCCAC
ACGGAGGAGGGGTGCCTGTCTGAGCACGCTGCCCTCGAGGAGGAGCTGCAACTGTGCAAG
GGGCTGGTCGAGGCACTCGAGACCAAGGTGACCCAGCAGGGGCTGAAGATGGTGGTGCCG
GACTGGACGGGGCCCAGATCCCCCCGGGACCCCTCACAGCAGGAACTGCCCCGGCTGTTG
TCGGCTGCCTGCAGGCTTCAGCTCAACGGGAACCTGCAGCTGGAGCTGGCGCAGGTGCTG
GCCCAGGAGAGGCCCAAGCTGCCAGAGGACCCTCTGCTCAGCGGCCTCCTGGACTCCCCG
GCACTCAAGGCCTGCCTGGACACTGCCGTGGAGAACATGCCCAGCCTGAAGATGAAGGTG
GTGGAGGTGCTGGCCGGCCACGGTCACCTGTATTCCCGCATCCCAGGCCTGCTCAGCCCC
CATCCCCTGCTGCAGCTGAGCTACACGGCCACCGACCGCCACCCCCAGGCCCTGGAGGCT
GCCCAGGCCGAGCTGCAGCAGCACGACGTTGCCCAGGGCCAGTGGGATCCCGCAGACCCT
GCCCCCAGCGCCCTGGGCAGCGCGGACCTCCTGGTGTGCAACTGTGCTGTGGCTGCCCTC
GGGGACCCGGCCTCAGCTCTCAGCAACATGGTGGCTGCCCTGAGAGAAGGGGGCTTTCTG
CTCCTGCACACACTGCTCCGGGGGCACCCTCGGGACATCGTGGCCTTCCTCACCTCCACT
GAGCCGCAGTATGGCCAGGGCATCCTGAGCCAGGACGCGTGGGAGAGCCTCTTCTCCAGG
GTGTCGCTGCGCCTGGTGGGCCTGAAGAAGTCCTTCTACGGCGCCACGCTCTTCCTGTGC
CGCCGGCCCACCCCGCAGGACAGCCCCATCTTCCTGCCGGTGGACGATACCAGCTTCCGC
TGGGTGGAGTCTCTGAAGGGCATCCTGGCTGACGAAGACTCTTCCCGGCCTGTGTGGCTG
AAGGCCATCAACTGTGCCACCTCGGGCGTGGTGGGCTTGGTGAACTGTCTCCGCCGAGAG
CCCGGCGGAACCGTCCGGTGTGTGCTGCTCTCCAACCTCAGCAGCACCTCCCACGTCCCG
GAGGTGGACCCGGGCTCCGCAGAACTGCAGAAGGTGTTGCAGGGAGACCTGGTGATGAAC
GTCTACCGCGACGGGGCCTGGGGGGTTTTCCGCCACTTCCTGCTGGAGGACAAGCCTGAG
GAGCCGACGGCACATGCCTTTGTGAGCACCCTCACCCGGGGGGACCTGTCCTCCATCCGC
TGGGTCTGCTCCTCGCTGCGCCATGCCCAGCCCACCTGCCCTGGCGCCCAGCTCTGCACG
GTCTACTACGCCTCCCTCAACTTCCGCGACATCATGCTGGCCACTGGCAAGCTGTCCCCT
GATGCCATCCCAGGGAAGTGGACCTCCCAGGACAGCCTGCTAGGTATGGAGTTCTCGGGC
CGAGACGCCAGCGGCAAGCGTGTGATGGGACTGGTGCCTGCCAAGGGCCTGGCCACCTCT
GTCCTGCTGTCACCGGACTTCCTCTGGGATGTGCCTTCCAACTGGACGCTGGAGGAGGCG
GCCTCGGTGCCTGTCGTCTACAGCACGGCCTACTACGCGCTGGTGGTGCGTGGGCGGGTG
CGCCCCGGGGAGACGCTGCTCATCCACTCGGGCTCGGGCGGCGTGGGCCAGGCCGCCATC
GCCATCGCCCTCAGTCTGGGCTGCCGCGTCTTCACCACCGTGGGGTCGGCTGAGAAGCGG
GCGTACCTCCAGGCCAGGTTCCCCCAGCTCGACAGCACCAGCTTCGCCAACTCCCGGGAC
ACATCCTTCGAGCAGCATGTGCTGTGGCACACGGGCGGGAAGGGCGTTGACCTGGTCTTG
AACTCCTTGGCGGAAGAGAAGCTGCAGGCCAGCGTGAGGTGCTTCGGTACGCACGGTCGC
TTCCTGGAAATTGGCAAATTCGACCTTTCTCAGAACCACCCGCTCGGCATGGCTATCTTC
CTGAAGAACGTGACATTCCACGGGGTCCTACTGGATGCGTTCTTCAACGAGAGCAGTGCT
GACTGGCGGGAGGTGTGGGCGCTTGTCGAGGCCGCCATCCGGGATGGGGTGGTACGGCCC
CTCAAGTGCACGGTGTTCCATGGGGCCCAGGTGGAGGACGCCTTCCGCTACATGGCCCAA
GGGAAGCACATTGGCAAAGTCGTCGTGCAGGTGCTTGCGGAGGAGCCGGCAGTGCTGAAG
GGGGCCAAACCCAAGCTGATGTCGGCCATCTCCAAGACCTTCTGCCCGGCCCACAAGAGC
TACATCATCGCTGGTGGTCTGGGTGGCTTCGGCCTGGAGTTGGCGCAGTGGCTGATACAG
CGTGGGGTGCAGAAGCTCGTGTTGACTTCTCGCTCCGGGATCCGGACAGGCTACCAGGCC
AAGCAGGTCCGCCGGTGGAGGCGCCAGGGGCTACAGGTGCAGGTGTCCACCAGCAACATC
AGCTCACTGGAGGGGGCCCGGGGCCTCATTGCCGAGGCGGCGCAGCTTGGGCCCGTGGGG
GGCGTCTTCAACCTGGCCGTGGTCTTGAGAGATGGCTTGCTGGAGAACCAGACCCCAGAG
TTCTTCCAGGACGTCTGCAAGCCCAAGTACAGCGGCACCCTGAACCTGGACAGGGTGACC
CGAGAGGCGTGCCCTGAGCTGGACTACTTTGTGGTCTTCTCCTCTGTGAGCTGCGGGCGT
GGCAATGCGGGACAGAGCAACTACGGCTTTGCCAATTCCGCCATGGAGCGTATCTGTGAG
AAACGCCGGCACGAAGGCCTCCCAGGCCTGGCCGTGCAGTGGGGCGCCATCGGCACCGTG
GGCATTTTGGTGGAGACGATGAGCACCAACGACACGATCGTCAGTGGCACGCTGCCCACG
CGCATTGGCGTCCTTGGCCTGGAGGTGCTGGACCTCTTCCTGAACCAGCCCCACATGGTC
CTGAGCAGCTTTGTGCTGGCTGAGAAGGCTGCGGCCTATAGGGACAGGGACAGCCAGCGG
GACCTGGTGGAGGCCGTGGCACACATCCTGGGCATCCGCGACTTGGCTGCTGTCAACCTG
GGCGGCTCACTGGCGGACCTGGGCCTGGACTCGCTCATGAGCGCGCCGGTGCGCCAGACG
CTGGAGCGTGAGCTCAACCTGGTGCTGTCCGTGCGCGAGGTGCGGCAACTCACGCTCCGG
AAACTGCAGGAGCTGTCCTCAAAGGCGGATGAAGCCAGCGAGCTGGCATGCCCCACGCCC
AAGGAGGATGGTCTGGCCCAGCAGCAGACTCAGCTGAACCTGCGCTCCCTGCTGGTGAAA
CCGGAGGGCCCCACCCTGATGCGGCTCAACTCCGTGCAGAGCTCGGAGCGGCCCCTGTTC
CTGGTGCACCCAATCGAGGCTACCACCGTGTTCCACAGCCTCGGTCCCGGTCTCAGCATC
CCCACCTATGGCCTGCAGTGCACCCCGGCTGCGCCCCTTGACAGCATCCACAGCCTGGCT
GCCTACTACATCGACTGCATCAGGCAGGTGCAGCCCGAGGGCCCCTACCGCGTGGCCGGC
TACTCCTACGGGGCCTGCGTGGCCTTTGAAATGTGCTCCCAGCTGCAGGCCCAGCAGAGC
CCAGCCCCCACCCACAACAGCCTCTTCCTGTTCGACGGCTCGCCCACCTACGTACTGGCC
TACACCCAGAGCTACCGGGCAAAGCTGACCCCAGGCTGTAAGGCTGAGGCTGAGACGGAG
GCCATATGCTTCTTCGTGCAGCAGTTCACGGACATGGAGCACAACAGGGTGCTGGAGGCG
CTGCTGCCGCTGAAGGGCCTAGAGGAGCGTGTGGCAGCCGCCGTGGACCTGATCATCAAG
AGCCACCAGGGCCTGGACCGCCAGGAGCTGAGCTTTGCGGCCCGGTCCTTCTACTACAGG
CTGCGTGCCGCTGACCAGTATACACCCAAGGCCAAGTACAGTGGCAACGTGATGCTACTG
CGGGCCAAGACGGGTGGCCGCTACGGCGAGGACCTGGGCGCGGACTACAACCTCTCCCAG
GTATGCGACGGGAAAGTATCCGTCCATATCATCGAGGGTGACCACCGCACGCTGCTGGAG
GGCAGCGGCCTGGAGTCCATCATCAGCATCATCCACAGCTCCCTGGCTGAGCCACGTGTG
AGTCGGGAGGGCTAG
Enzyme 1 GenBank Gene ID U26644 Link Image
Enzyme 1 GeneCard ID FASN Link Image
Enzyme 1 GenAtlas ID FASN Link Image
Enzyme 1 HGNC ID HGNC:3594 Link Image
Enzyme 1 Chromosome Location 17
Enzyme 1 Locus 17q25
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Jayakumar A, Tai MH, Huang WY, al-Feel W, Hsu M, Abu-Elheiga L, Chirala SS, Wakil SJ: Human fatty acid synthase: properties and molecular cloning. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8695-9. [PubMed Link Image]
  2. Kuhajda FP, Jenner K, Wood FD, Hennigar RA, Jacobs LB, Dick JD, Pasternack GR: Fatty acid synthesis: a potential selective target for antineoplastic therapy. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6379-83. [PubMed Link Image]
  3. Semenkovich CF, Coleman T, Fiedorek FT Jr: Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation. J Lipid Res. 1995 Jul;36(7):1507-21. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5287
Enzyme 2 Name Calcium-dependent phospholipase A2 precursor
Enzyme 2 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase
  2. PLA2-10
  3. Group V phospholipase A2
Enzyme 2 Gene Name PLA2G5
Enzyme 2 Protein Sequence >Calcium-dependent phospholipase A2 precursor
MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGT
DWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKR
NLRSYNPQYQYFPNILCS
Enzyme 2 Number of Residues 138
Enzyme 2 Molecular Weight 15674
Enzyme 2 Theoretical pI 8.48
Enzyme 2 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. This isozyme hydrolyzes more efficiently L-alpha-1-palmitoyl-2-oleoyl phosphatidylcholine than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L- alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine, or L- alpha-1-stearoyl-2-arachidonyl phosphatidylinositol. May be involved in the production of lung surfactant, the remodeling or regulation of cardiac muscle
Enzyme 2 Pathways
Enzyme 2 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-20
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 460915 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P39877 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PA2G5_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >417 bp
ATGAAAGGCCTCCTCCCACTGGCTTGGTTCCTGGCTTGTAGTGTGCCTGCTGTGCAAGGA
GGCTTGCTGGACCTAAAATCAATGATCGAGAAGGTGACAGGGAAGAACGCCCTGACAAAC
TACGGCTTCTACGGCTGTTACTGCGGCTGGGGCGGCCGAGGAACCCCCAAGGATGGCACC
GATTGGTGCTGTTGGGCGCATGACCACTGCTATGGGCGGCTGGAGGAGAAGGGCTGCAAC
ATTCGCACACAGTCCTACAAATACAGATTCGCGTGGGGCGTGGTCACCTGCGAGCCCGGG
CCCTTCTGCCATGTGAACCTCTGTGCCTGTGACCGGAAGCTCGTCTACTGCCTCAAGAGA
AACCTACGGAGCTACAACCCACAGTACCAATACTTTCCCAACATCCTCTGCTCCTAG
Enzyme 2 GenBank Gene ID U03090 Link Image
Enzyme 2 GeneCard ID PLA2G5 Link Image
Enzyme 2 GenAtlas ID PLA2G5 Link Image
Enzyme 2 HGNC ID HGNC:9038 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p36-p34
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Chen J, Engle SJ, Seilhamer JJ, Tischfield JA: Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2. J Biol Chem. 1994 Jan 28;269(4):2365-8. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5288
Enzyme 3 Name Group IIF secretory phospholipase A2 precursor
Enzyme 3 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIIF
  2. GIIF sPLA2
  3. sPLA(2-IIF
Enzyme 3 Gene Name PLA2G2F
Enzyme 3 Protein Sequence >Group IIF secretory phospholipase A2 precursor
MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEV
DWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLC
LMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP
Enzyme 3 Number of Residues 168
Enzyme 3 Molecular Weight 18658
Enzyme 3 Theoretical pI 4.94
Enzyme 3 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference
Enzyme 3 Pathways
Enzyme 3 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-20
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 12276060 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9BZM2 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PA2GF_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >507 bp
ATGAAGAAGTTCTTCACCGTGGCCATCCTTGCTGGCAGCGTTCTGTCCACAGCTCACGGC
AGCCTGCTCAACCTGAAGGCCATGGTGGAGGCCGTCACAGGGAGGAGCGCCATCCTGTCC
TTCGTGGGCTACGGTTGCTACTGTGGGCTGGGGGGCCGTGGCCAGCCCAAGGATGAGGTG
GACTGGTGCTGCCACGCCCACGACTGCTGCTACCAGGAACTCTTTGACCAAGGCTGTCAC
CCCTATGTGGACCACTATGATCACACCATCGAGAACAACACTGAGATAGTCTGCAGTGAC
CTCAACAAGACAGAGTGTGACAAGCAGACATGCATGTGTGACAAGAACATGGTTCTGTGC
CTCATGAACCAGACGTACCGAGAGGAGTACCGTGGCTTCCTCAATGTCTACTGCCAGGGC
CCCACGCCCAACTGCAGCATCTATGAACCGCCCCCTGAGGAGGTCACCTGCAGTCACCAA
TCCCCAGCGCCCCCCGCCCCTCCCTAG
Enzyme 3 GenBank Gene ID AF306566 Link Image
Enzyme 3 GeneCard ID PLA2G2F Link Image
Enzyme 3 GenAtlas ID PLA2G2F Link Image
Enzyme 3 HGNC ID HGNC:30040 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p35
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Valentin E, Singer AG, Ghomashchi F, Lazdunski M, Gelb MH, Lambeau G: Cloning and recombinant expression of human group IIF-secreted phospholipase A(2). Biochem Biophys Res Commun. 2000 Dec 9;279(1):223-8. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5289
Enzyme 4 Name Cytosolic phospholipase A2
Enzyme 4 Synonyms
  1. cPLA2
  2. Phospholipase A2 group IVA[Includes: Phospholipase A2
  3. Phosphatidylcholine 2- acylhydrolase
  4. Lysophospholipase
Enzyme 4 Gene Name PLA2G4A
Enzyme 4 Protein Sequence >Cytosolic phospholipase A2
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA
Enzyme 4 Number of Residues 749
Enzyme 4 Molecular Weight 85212
Enzyme 4 Theoretical pI 5.03
Enzyme 4 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase activity
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid catabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response
Enzyme 4 Pathways
Enzyme 4 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 190007 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P47712 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PA24A_HUMAN Link Image
Enzyme 4 PDB ID 1CJY Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2250 bp
ATGTCATTTATAGATCCTTACCAGCACATTATAGTGGAGCACCAGTATTCCCACAAGTTT
ACGGTAGTGGTGTTACGTGCCACCAAAGTGACAAAGGGGGCCTTTGGTGACATGCTTGAT
ACTCCAGATCCCTATGTGGAACTTTTTATCTCTACAACCCCTGACAGCAGGAAGAGAACA
AGACATTTCAATAATGACATAAACCCTGTGTGGAATGAGACCTTTGAATTTATTTTGGAT
CCTAATCAGGAAAATGTTTTGGAGATTACGTTAATGGATGCCAATTATGTCATGGATGAA
ACTCTAGGGACAGCAACATTTACTGTATCTTCTATGAAGGTGGGAGAAAAGAAAGAAGTT
CCTTTTATTTTCAACCAAGTCACTGAAATGGTTCTAGAAATGTCTCTTGAAGTTTGCTCA
TGCCCAGACCTACGATTTAGTATGGCTCTGTGTGATCAGGAGAAGACTTTCAGACAACAG
AGAAAAGAACACATAAGGGAGAGCATGAAGAAACTCTTGGGTCCAAAGAATAGTGAAGGA
TTGCATTCTGCACGTGATGTGCCTGTGGTAGCCATATTGGGTTCAGGTGGGGGTTTCCGA
GCCATGGTGGGATTCTCTGGTGTGATGAAGGCATTATACGAATCAGGAATTCTGGATTGT
GCTACCTACGTTGCTGGTCTTTCTGGCTCCACCTGGTATATGTCAACCTTGTATTCTCAC
CCTGATTTTCCAGAGAAAGGGCCAGAGGAGATTAATGAAGAACTAATGAAAAATGTTAGC
CACAATCCCCTTTTACTTCTCACACCACAGAAAGTTAAAAGATATGTTGAGTCTTTATGG
AAGAAGAAAAGCTCTGGACAACCTGTCACCTTTACTGATATCTTTGGGATGTTAATAGGA
GAAACACTAATTCATAATAGAATGAATACTACTCTGAGCAGTTTGAAGGAAAAAGTTAAT
ACTGCACAATGCCCTTTACCTCTTTTCACCTGTCTTCATGTCAAACCTGACGTTTCAGAG
CTGATGTTTGCAGATTGGGTTGAATTTAGTCCATACGAAATTGGCATGGCTAAATATGGT
ACTTTTATGGCTCCCGACTTATTTGGAAGCAAATTTTTTATGGGAACAGTCGTTAAGAAG
TATGAAGAAAACCCCTTGCATTTCTTAATGGGTGTCTGGGGCAGTGCCTTTTCCATATTG
TTCAACAGAGTTTTGGGCGTTTCTGGTTCACAAAGCAGAGGCTCCACAATGGAGGAAGAA
TTAGAAAATATTACCACAAAGCATATTGTGAGTAATGATAGCTCGGACAGTGATGATGAA
TCACACGAACCCAAAGGCACTGAAAATGAAGATGCTGGAAGTGACTATCAAAGTGATAAT
CAAGCAAGTTGGATTCATCGTATGATAATGGCCTTGGTGAGTGATTCAGCTTTATTCAAT
ACCAGAGAAGGACGTGCTGGGAAGGTACACAACTTCATGCTGGGCTTGAATCTCAATACA
TCTTATCCACTGTCTCCTTTGAGTGACTTTGCCACACAGGACTCCTTTGATGATGATGAA
CTGGATGCAGCTGTAGCAGATCCTGATGAATTTGAGCGAATATATGAGCCTCTGGATGTC
AAAAGTAAAAAGATTCATGTAGTGGACAGTGGGCTCACATTTAACCTGCCGTATCCCTTG
ATACTGAGACCTCAGAGAGGGGTTGATCTCATAATCTCCTTTGACTTTTCTGCAAGGCCA
AGTGACTCTAGTCCTCCGTTCAAGGAACTTCTACTTGCAGAAAAGTGGGCTAAAATGAAC
AAGCTCCCCTTTCCAAAGATTGATCCTTATGTGTTTGATCGGGAAGGGCTGAAGGAGTGC
TATGTCTTTAAACCCAAGAATCCTGATATGGAGAAAGATTGCCCAACCATCATCCACTTT
GTTCTGGCCAACATCAACTTCAGAAAGTACAAGGCTCCAGGTGTTCCAAGGGAAACTGAG
GAAGAGAAAGAAATCGCTGACTTTGATATTTTTGATGACCCAGAATCACCATTTTCAACC
TTCAATTTTCAATATCCAAATCAAGCATTCAAAAGACTACATGATCTTATGCACTTCAAT
ACTCTGAACAACATTGATGTGATAAAAGAAGCCATGGTTGAAAGCATTGAATATAGAAGA
CAGAATCCATCTCGTTGCTCTGTTTCCCTTAGTAATGTTGAGGCAAGAAGATTTTTCAAC
AAGGAGTTTCTAAGTAAACCCAAAGCATAG
Enzyme 4 GenBank Gene ID M72393 Link Image
Enzyme 4 GeneCard ID PLA2G4A Link Image
Enzyme 4 GenAtlas ID PLA2G4A Link Image
Enzyme 4 HGNC ID HGNC:9035 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1q25
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Clark JD, Lin LL, Kriz RW, Ramesha CS, Sultzman LA, Lin AY, Milona N, Knopf JL: A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP. Cell. 1991 Jun 14;65(6):1043-51. [PubMed Link Image]
  2. Sharp JD, White DL, Chiou XG, Goodson T, Gamboa GC, McClure D, Burgett S, Hoskins J, Skatrud PL, Sportsman JR, et al.: Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2. J Biol Chem. 1991 Aug 15;266(23):14850-3. [PubMed Link Image]
  3. Lin LL, Wartmann M, Lin AY, Knopf JL, Seth A, Davis RJ: cPLA2 is phosphorylated and activated by MAP kinase. Cell. 1993 Jan 29;72(2):269-78. [PubMed Link Image]
  4. Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV: PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. Mol Cell Biol. 2001 Jul;21(14):4470-81. [PubMed Link Image]
  5. Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL: Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J Biol Chem. 1998 Jan 16;273(3):1596-604. [PubMed Link Image]
  6. Xu GY, McDonagh T, Yu HA, Nalefski EA, Clark JD, Cumming DA: Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2. J Mol Biol. 1998 Jul 17;280(3):485-500. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5290
Enzyme 5 Name Phospholipase A2 precursor
Enzyme 5 Synonyms
  1. Phosphatidylcholine 2- acylhydrolase
  2. Group IB phospholipase A2
Enzyme 5 Gene Name PLA2G1B
Enzyme 5 Protein Sequence >Phospholipase A2 precursor
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPV
DELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNC
DRNAAICFSKAPYNKAHKNLDTKKYCQS
Enzyme 5 Number of Residues 148
Enzyme 5 Molecular Weight 16360
Enzyme 5 Theoretical pI 7.91
Enzyme 5 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides
Enzyme 5 Pathways
Enzyme 5 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-15
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 387025 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P04054 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PA21B_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >447 bp
ATGAAACTCCTTGTGCTAGCTGTGCTGCTCACAGTGGCCGCCGCCGACAGCGGCATCAGC
CCTCGGGCCGTGTGGCAGTTCCGCAAAATGATCAAGTGCGTGATCCCGGGGAGTGACCCC
TTCTTGGAATACAACAACTACGGCTGCTACTGTGGCTTGGGGGGCTCAGGCACCCCCGTG
GATGAACTGGACAAGTGCTGCCAGACACATGACAACTGCTACGACCAGGCCAAGAAGCTG
GACAGCTGTAAATTTCTGCTGGACAACCCGTACACCCACACCTATTCATACTCGTGCTCT
GGCTCGGCAATCACCTGTAGCAGCAAAAACAAAGAGTGTGAGGCCTTCATTTGCAACTGC
GACCGCAACGCTGCCATCTGCTTTTCAAAAGCTCCATATAACAAGGCACACAAGAACCTG
GACACCAAGAAGTATTGTCAGAGTTGA
Enzyme 5 GenBank Gene ID M21056 Link Image
Enzyme 5 GeneCard ID PLA2G1B Link Image
Enzyme 5 GenAtlas ID PLA2G1B Link Image
Enzyme 5 HGNC ID HGNC:9030 Link Image
Enzyme 5 Chromosome Location 12
Enzyme 5 Locus 12q23-q24.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK: Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung. DNA. 1986 Dec;5(6):519-27. [PubMed Link Image]
  2. Grataroli R, Dijkman R, Dutilh CE, van der Ouderaa F, De Haas GH, Figarella C: Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region. Eur J Biochem. 1982 Feb;122(1):111-7. [PubMed Link Image]
  3. Verheij HM, Westerman J, Sternby B, De Haas GH: The complete primary structure of phospholipase A2 from human pancreas. Biochim Biophys Acta. 1983 Sep 14;747(1-2):93-9. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5292
Enzyme 6 Name Group 10 secretory phospholipase A2 precursor
Enzyme 6 Synonyms
  1. Group X secretory phospholipase A2
  2. Phosphatidylcholine 2-acylhydrolase GX
  3. GX sPLA2
  4. sPLA2-X
Enzyme 6 Gene Name PLA2G10
Enzyme 6 Protein Sequence >Group 10 secretory phospholipase A2 precursor
MLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPIAYMKYGCFCG
LGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGPAENKCQELLC
KCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
Enzyme 6 Number of Residues 155
Enzyme 6 Molecular Weight 17132
Enzyme 6 Theoretical pI 6.46
Enzyme 6 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine
Enzyme 6 Pathways
Enzyme 6 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-21
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 2289237 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O15496 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PA2GX_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >498 bp
ATGGGGCCGCTACCTGTGTGCCTGCCAATCATGCTGCTCCTGCTACTGCCGTCGCTGCTG
CTGCTGCTGCTTCTACCTGGCCCCGGGTCCGGCGAGGCCTCCAGGATATTACGTGTGCAC
CGGCGTGGGATCCTGGAACTGGCAGGAACTGTGGGTTGTGTTGGTCCCCGAACCCCCATC
GCCTATATGAAATATGGTTGCTTTTGTGGCTTGGGAGGCCATGGCCAGCCCCGCGATGCC
ATTGACTGGTGCTGCCATGGCCACGACTGTTGTTACACTCGAGCTGAGGAGGCCGGCTGC
AGCCCCAAGACAGAGCGCTACTCCTGGCAGTGCGTCAATCAGAGCGTCCTGTGCGGACCG
GCAGAGAACAAATGCCAAGAACTGTTGTGCAAGTGTGACCAGGAGATTGCTAACTGCTTA
GCCCAAACTGAGTACAACTTAAAGTACCTCTTCTACCCCCAGTTCCTATGTGAGCCGGAC
TCGCCCAAGTGTGACTGA
Enzyme 6 GenBank Gene ID U95301 Link Image
Enzyme 6 GeneCard ID PLA2G10 Link Image
Enzyme 6 GenAtlas ID PLA2G10 Link Image
Enzyme 6 HGNC ID HGNC:9029 Link Image
Enzyme 6 Chromosome Location 16
Enzyme 6 Locus 16p13.1-p12
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Cupillard L, Koumanov K, Mattei MG, Lazdunski M, Lambeau G: Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. J Biol Chem. 1997 Jun 20;272(25):15745-52. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5293
Enzyme 7 Name Galactoside-binding soluble lectin 13
Enzyme 7 Synonyms
  1. Placental tissue protein 13
  2. Placenta protein 13
  3. PP13
  4. Galectin-13
Enzyme 7 Gene Name LGALS13
Enzyme 7 Protein Sequence >Galactoside-binding soluble lectin 13
MSSLPVPYKLPVSLSVGSCVIIKGTPIHSFINDPQLQVDFYTDMDEDSDIAFRFRVHFGN
HVVMNRREFGIWMLEETTDYVPFEDGKQFELCIYVHYNEYEIKVNGIRIYGFVHRIPPSF
VKMVQVSRDISLTSVCVCN
Enzyme 7 Number of Residues 139
Enzyme 7 Molecular Weight 16119
Enzyme 7 Theoretical pI 5.53
Enzyme 7 GO Classification
Function
  • binding
  • carbohydrate binding
  • sugar binding
Process
Component
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Has lysophospholipase activity
Enzyme 7 Pathways
Enzyme 7 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 6650760 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9UHV8 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PP13_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >420 bp
ATGTCTTCTTTACCCGTGCCATACAAACTGCCTGTGTCTTTGTCTGTTGGTTCCTGCGTG
ATAATCAAAGGGACACCAATCCACTCTTTTATCAATGACCCACAGCTGCAGGTGGATTTC
TACACTGACATGGATGAGGATTCAGATATTGCCTTCCGTTTCCGAGTGCACTTTGGCAAT
CATGTGGTCATGAACAGGCGTGAGTTTGGGATATGGATGTTGGAGGAGACAACAGACTAC
GTGCCCTTTGAGGATGGCAAACAATTTGAGCTGTGCATCTACGTACATTACAATGAGTAT
GAGATAAAGGTCAATGGCATACGCATTTACGGCTTTGTCCATCGAATCCCGCCATCATTT
GTGAAGATGGTGCAAGTGTCGAGAGATATCTCCCTGACCTCAGTGTGTGTCTGCAATTGA
Enzyme 7 GenBank Gene ID AF117383 Link Image
Enzyme 7 GeneCard ID LGALS13 Link Image
Enzyme 7 GenAtlas ID LGALS13 Link Image
Enzyme 7 HGNC ID HGNC:15449 Link Image
Enzyme 7 Chromosome Location 19
Enzyme 7 Locus 19q13.1
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Than NG, Sumegi B, Than GN, Berente Z, Bohn H: Isolation and sequence analysis of a cDNA encoding human placental tissue protein 13 (PP13), a new lysophospholipase, homologue of human eosinophil Charcot-Leyden Crystal protein. Placenta. 1999 Nov;20(8):703-10. [PubMed Link Image]
  2. Bohn H, Kraus W, Winckler W: Purification and characterization of two new soluble placental tissue proteins (PP13 and PP17). Oncodev Biol Med. 1983;4(5):343-50. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5294
Enzyme 8 Name Group IIE secretory phospholipase A2 precursor
Enzyme 8 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIIE
  2. GIIE sPLA2
  3. sPLA(2-IIE
Enzyme 8 Gene Name PLA2G2E
Enzyme 8 Protein Sequence >Group IIE secretory phospholipase A2 precursor
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC
Enzyme 8 Number of Residues 142
Enzyme 8 Molecular Weight 15989
Enzyme 8 Theoretical pI 8.28
Enzyme 8 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids
Enzyme 8 Pathways
Enzyme 8 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-19
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 7108923 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9NZK7 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PA2GE_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >429 bp
ATGAAATCTCCCCACGTGCTGGTGTTCCTTTGCCTCCTGGTGGCTCTGGTCACCGGGAAC
CTGGTTCAGTTTGGGGTGATGATCGAGAAGATGACAGGCAAGTCCGCCCTGCAGTACAAC
GACTATGGCTGTTACTGCGGCATCGGTGGCTCCCACTGGCCGGTGGACCAGACTGACTGG
TGCTGCCACGCCCACGACTGCTGCTACGGGCGTCTGGAGAAGCTGGGCTGTGAGCCCAAA
CTGGAAAAGTATCTTTTCTCTGTCAGCGAACGTGGCATTTTCTGCGCCGGCAGGACCACC
TGCCAGCGGCTGACCTGCGAGTGTGACAAGAGGGCTGCCCTCTGCTTTCGCCGCAACCTG
GGCACCTACAACCGCAAATATGCCCATTATCCCAACAAGCTGTGCACCGGGCCCACCCCG
CCCTGCTGA
Enzyme 8 GenBank Gene ID AF189279 Link Image
Enzyme 8 GeneCard ID PLA2G2E Link Image
Enzyme 8 GenAtlas ID PLA2G2E Link Image
Enzyme 8 HGNC ID HGNC:13414 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1p36.13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Suzuki N, Ishizaki J, Yokota Y, Higashino K, Ono T, Ikeda M, Fujii N, Kawamoto K, Hanasaki K: Structures, enzymatic properties, and expression of novel human and mouse secretory phospholipase A(2)s. J Biol Chem. 2000 Feb 25;275(8):5785-93. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5296
Enzyme 9 Name Group XIIA secretory phospholipase A2 precursor
Enzyme 9 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GXII
  2. GXII sPLA2
Enzyme 9 Gene Name PLA2G12A
Enzyme 9 Protein Sequence >Group XIIA secretory phospholipase A2 precursor
MALLSRPALTLLLLLMAAVVRCQEQAQTTDWRATLKTIRNGVHKIDTYLNAALDLLGGED
GLCQYKCSDGSKPFPRYGYKPSPPNGCGSPLFGVHLNIGIPSLTKCCNQHDRCYETCGKS
KNDCDEEFQYCLSKICRDVQKTLGLTQHVQACETTVELLFDSVIHLGCKPYLDSQRAACR
CHYEEKTDL
Enzyme 9 Number of Residues 189
Enzyme 9 Molecular Weight 21067
Enzyme 9 Theoretical pI 7.27
Enzyme 9 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
  • extracellular region
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides
Enzyme 9 Pathways
Enzyme 9 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-22
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 12276062 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9BZM1 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PG12A_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >570 bp
ATGGCCCTGCTCTCGCGCCCCGCGCTCACCCTCCTGCTCCTCCTCATGGCCGCTGTTGTC
AGGTGCCAGGAGCAGGCCCAGACCACCGACTGGAGAGCCACCCTGAAGACCATCCGGAAC
GGCGTTCATAAGATAGACACGTACCTGAACGCCGCCTTGGACCTCCTGGGAGGCGAGGAC
GGTCTCTGCCAGTATAAATGCAGTGACGGATCTAAGCCTTTCCCACGTTATGGTTATAAA
CCCTCCCCACCGAATGGATGTGGCTCTCCACTGTTTGGTGTTCATCTTAACATTGGTATC
CCTTCCCTGACAAAGTGTTGCAACCAACACGACAGGTGCTATGAGACCTGTGGCAAAAGC
AAGAATGACTGTGATGAAGAATTCCAGTATTGCCTCTCCAAGATCTGCCGAGATGTACAG
AAAACACTAGGACTAACTCAGCATGTTCAGGCATGTGAAACAACAGTGGAGCTCTTGTTT
GACAGTGTTATACATTTAGGTTGTAAACCATATCTGGACAGCCAACGAGCCGCATGCAGG
TGTCATTATGAAGAAAAAACTGATCTTTAA
Enzyme 9 GenBank Gene ID AF306567 Link Image
Enzyme 9 GeneCard ID PLA2G12A Link Image
Enzyme 9 GenAtlas ID PLA2G12A Link Image
Enzyme 9 HGNC ID HGNC:18554 Link Image
Enzyme 9 Chromosome Location 4
Enzyme 9 Locus 4q25
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Gelb MH, Valentin E, Ghomashchi F, Lazdunski M, Lambeau G: Cloning and recombinant expression of a structurally novel human secreted phospholipase A2. J Biol Chem. 2000 Dec 22;275(51):39823-6. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5297
Enzyme 10 Name 85 kDa calcium-independent phospholipase A2
Enzyme 10 Synonyms
  1. iPLA2
  2. CaI- PLA2
  3. Group VI phospholipase A2
  4. GVI PLA2
Enzyme 10 Gene Name PLA2G6
Enzyme 10 Protein Sequence >85 kDa calcium-independent phospholipase A2
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLV
NPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSW
SVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMD
VTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLL
LCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMA
RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK
DNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLRTVGAEYCFPPIHG
VPAEQGSAAPHHPFSLERAQPPPISLNNLELQDLMHISRARKPAFILGSMRDEKRTHDHL
LCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGM
YFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFR
NYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNP
TLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKT
VFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVN
ALWETEVYIYEHREEFQKLIQLLLSP
Enzyme 10 Number of Residues 806
Enzyme 10 Molecular Weight 89904
Enzyme 10 Theoretical pI 7.28
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity
Enzyme 10 Pathways
Enzyme 10 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 3142700 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O60733 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PA2G6_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >2421 bp
ATGCAGTTCTTTGGCCGCCTGGTCAATACCTTCAGTGGCGTCACCAACTTGTTCTCTAAC
CCATTCCGGGTGAAGGAGGTGGCTGTGGCCGACTACACCTCGAGTGACCGAGTTCGGGAG
GAAGGGCAGCTGATTCTGTTCCAGAACACTCCCAACCGCACCTGGGACTGCGTCCTGGTC
AACCCCAGGAACTCACAGAGTGGATTCCGACTCTTCCAGCTGGAGTTGGAGGCTGACGCC
CTAGTGAATTTCCATCAGTATTCTTCCCAGCTGCTACCCTTCTATGAGAGCTCCCCTCAG
GTCCTGCACACTGAGGTCCTGCAGCACCTGACCGACCTCATCCGTAACCACCCCAGCTGG
TCAGTGGCCCACCTGGCTGTGGAGCTAGGGATCCGCGAGTGCTTCCATCACAGCCGTATC
ATCAGCTGTGCCAATTGCGCGGAGAACGAGGAGGGCTGCACACCCCTGCACCTGGCCTGC
CGCAAGGGTGATGGGGAGATCCTGGTGGAGCTGGTGCAGTACTGCCACACTCAGATGGAT
GTCACCGACTACAAGGGAGAGACCGTCTTCCATTATGCTGTCCAGGGTGACAATTCTCAG
GTGCTGCAGCTCCTTGGAAGGAACGCAGTGGCTGGCCTGAACCAGGTGAATAACCAAGGG
CTGACCCCGCTGCACCTGGCCTGCCAGCTGGGGAAGCAGGAGATGGTCCGCGTGCTGCTG
CTGTGCAATGCTCGGTGCAACATCATGGGCCCCAACGGCTACCCCATCCACTCGGCCATG
AAGTTCTCTCAGAAGGGGTGTGCGGAGATGATCATCAGCATGGACAGCAGCCAGATCCAC
AGCAAAGACCCCCGTTACGGAGCCAGCCCCCTCCACTGGGCCAAGAACGCAGAGATGGCC
CGCATGCTGCTGAAACGGGGCTGCAACGTGAACAGCACCAGCTCCGCGGGGAACACGGCC
CTGCACGTGGCGGTGATGCGCAACCGCTTCGACTGTGCCATAGTGCTGCTGACCCACGGG
GCCAACGCGGATGCCCGCGGAGAGCACGGCAACACCCCGCTGCACCTGGCCATGTCGAAA
GACAACGTGGAGATGATCAAGGCCCTCATCGTGTTCGGAGCAGAAGTGGACACCCCGAAT
GACTTTGGGGAGACTCCTACATTCCTAGCCTCCAAAATCGGCAGACTTGTCACCAGGAAG
GCGATCTTGACTCTGCTGAGAACCGTGGGGGCCGAATACTGCTTCCCACCCATCCACGGG
GTCCCCGCGGAGCAGGGCTCTGCAGCGCCACATCATCCCTTCTCCCTGGAAAGAGCTCAG
CCCCCACCGATCAGCCTAAACAACCTAGAACTACAGGATCTCATGCACATCTCACGGGCC
CGGAAGCCAGCGTTCATCCTGGGCTCCATGAGGGACGAGAAGCGGACCCACGACCACCTG
CTGTGCCTGGATGGAGGAGGAGTGAAAGGCCTCATCATCATCCAGCTCCTCATCGCCATC
GAGAAGGCCTCGGGTGTGGCCACCAAGGACCTGTTTGACTGGGTGGCGGGCACCAGCACT
GGAGGCATCCTGGCCCTGGCCATTCTGCACAGTAAGTCCATGGCCTACATGCGCGGCATG
TACTTTCGCATGAAGGATGAGGTGTTCCGGGGCTCCAGGCCCTACGAGTCGGGGCCCCTG
GAGGAGTTCCTGAAGCGGGAGTTTGGGGAGCACACCAAGATGACGGACGTCAGGAAACCC
AAGGTGATGCTGACAGGGACACTGTCTGACCGGCAGCCGGCTGAACTCCACCTCTTCCGG
AACTACGATGCTCCAGAAACTGTCCGGGAGCCTCGTTTCAACCAGAACGTTAACCTCAGG
CCTCCAGCTCAGCCCTCAGACCAGCTGGTGTGGCGGGCGGCCCGAAGCAGCGGGGCAGCT
CCTACTTACTTCCGACCCAATGGGCGCTTCCTGGACGGTGGGCTGCTGGCCAACAACCCC
ACGCTGGATGCCATGACCGAGATCCATGAGTACAATCAGGACCTGATCCGCAAGGGTCAG
GCCAACAAGGTGAAGAAACTCTCCATCGTTGTCTCCCTGGGGACAGGGAGGTCCCCACAA
GTGCCTGTGACCTGTGTGGATGTCTTCCGTCCCAGCAACCCCTGGGAGCTGGCCAAGACT
GTTTTTGGGGCCAAGGAACTGGGCAAGATGGTGGTGGACTGTTGCACGGATCCAGACGGG
CGGGCTGTGGACCGGGCACGGGCCTGGTGCGAGATGGTCGGCATCCAGTACTTCAGATTG
AACCCCCAGCTGGGGACGGACATCATGCTGGATGAGGTCAGTGACACAGTGCTGGTCAAC
GCCCTCTGGGAGACCGAGGTCTACATCTATGAGCACCGCGAGGAGTTCCAGAAGCTCATC
CACCTGCTGCTCTCACCCTGA
Enzyme 10 GenBank Gene ID AF064594 Link Image
Enzyme 10 GeneCard ID PLA2G6 Link Image
Enzyme 10 GenAtlas ID PLA2G6 Link Image
Enzyme 10 HGNC ID HGNC:9039 Link Image
Enzyme 10 Chromosome Location 22
Enzyme 10 Locus 22q13.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Larsson PK, Claesson HE, Kennedy BP: Multiple splice variants of the human calcium-independent phospholipase A2 and their effect on enzyme activity. J Biol Chem. 1998 Jan 2;273(1):207-14. [PubMed Link Image]
  2. Ma Z, Wang X, Nowatzke W, Ramanadham S, Turk J: Human pancreatic islets express mRNA species encoding two distinct catalytically active isoforms of group VI phospholipase A2 (iPLA2) that arise from an exon-skipping mechanism of alternative splicing of the transcript from the iPLA2 gene on chromosome 22q13.1. J Biol Chem. 1999 Apr 2;274(14):9607-16. [PubMed Link Image]
  3. Larsson Forsell PK, Kennedy BP, Claesson HE: The human calcium-independent phospholipase A2 gene multiple enzymes with distinct properties from a single gene. Eur J Biochem. 1999 Jun;262(2):575-85. [PubMed Link Image]
  4. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5299
Enzyme 11 Name Eosinophil lysophospholipase
Enzyme 11 Synonyms
  1. Charcot-Leyden crystal protein
  2. Lysolecithin acylhydrolase
  3. CLC
  4. Galectin-10
Enzyme 11 Gene Name CLC
Enzyme 11 Protein Sequence >Eosinophil lysophospholipase
MSLLPVPYTEAASLSTGSTVTIKGRPLVCFLNEPYLQVDFHTEMKEESDIVFHFQVCFGR
RVVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEA
VKMVQVWRDISLTKFNVSYLKR
Enzyme 11 Number of Residues 142
Enzyme 11 Molecular Weight 16481
Enzyme 11 Theoretical pI 7.50
Enzyme 11 GO Classification
Function
  • binding
  • carbohydrate binding
  • sugar binding
Process
Component
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function May have both lysophospholipase and carbohydrate-binding activities
Enzyme 11 Pathways
Enzyme 11 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 187274 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q05315 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name LPPL_HUMAN Link Image
Enzyme 11 PDB ID 1QKQ Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >429 bp
ATGTCCCTGCTACCCGTGCCATACACAGAGGCTGCCTCTTTGTCTACTGGTTCTACTGTG
ACAATCAAAGGGCGACCACTTGTCTGTTTCTTGAATGAACCATATCTGCAGGTGGATTTC
CACACTGAGATGAAGGAGGAATCAGACATTGTCTTCCATTTCCAAGTGTGCTTTGGTCGT
CGTGTGGTCATGAACAGCCGTGAGTATGGGGCCTGGAAGCAGCAGGTGGAATCCAAGAAC
ATGCCCTTTCAGGATGGCCAAGAATTTGAACTGAGCATCTCAGTGCTGCCAGATAAGTAC
CAGGTAATGGTCAATGGCCAATCCTCTTACACCTTTGACCATAGAATCAAGCCTGAGGCT
GTGAAGATGGTGCAAGTGTGGAGAGATATCTCCCTGACCAAATTTAATGTCAGCTATTTA
AAGAGATAA
Enzyme 11 GenBank Gene ID L01664 Link Image
Enzyme 11 GeneCard ID CLC Link Image
Enzyme 11 GenAtlas ID CLC Link Image
Enzyme 11 HGNC ID HGNC:2014 Link Image
Enzyme 11 Chromosome Location 19
Enzyme 11 Locus 19q13.1
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Ackerman SJ, Corrette SE, Rosenberg HF, Bennett JC, Mastrianni DM, Nicholson-Weller A, Weller PF, Chin DT, Tenen DG: Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily. J Immunol. 1993 Jan 15;150(2):456-68. [PubMed Link Image]
  2. Mastrianni DM, Eddy RL, Rosenberg HF, Corrette SE, Shows TB, Tenen DG, Ackerman SJ: Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14. Genomics. 1992 May;13(1):240-2. [PubMed Link Image]
  3. Dyer KD, Handen JS, Rosenberg HF: The genomic structure of the human Charcot-Leyden crystal protein gene is analogous to those of the galectin genes. Genomics. 1997 Mar 1;40(2):217-21. [PubMed Link Image]
  4. Leonidas DD, Elbert BL, Zhou Z, Leffler H, Ackerman SJ, Acharya KR: Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. Structure. 1995 Dec 15;3(12):1379-93. [PubMed Link Image]
  5. Swaminathan GJ, Leonidas DD, Savage MP, Ackerman SJ, Acharya KR: Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution. Biochemistry. 1999 Oct 19;38(42):13837-43. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5301
Enzyme 12 Name Phospholipase A2, membrane associated precursor
Enzyme 12 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase
  2. Group IIA phospholipase A2
  3. GIIC sPLA2
  4. Non-pancreatic secretory phospholipase A2
  5. NPS-PLA2
Enzyme 12 Gene Name PLA2G2A
Enzyme 12 Protein Sequence >Phospholipase A2, membrane associated precursor
MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDAT
DRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFAR
NKTTYNKKYQYYSNKHCRGSTPRC
Enzyme 12 Number of Residues 144
Enzyme 12 Molecular Weight 16083
Enzyme 12 Theoretical pI 9.51
Enzyme 12 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Thought to participate in the regulation of the phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides
Enzyme 12 Pathways
Enzyme 12 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-20
Enzyme 12 Transmembrane Regions Not Available
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 190889 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P14555 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PA2GA_HUMAN Link Image
Enzyme 12 PDB ID 1DB4 Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >435 bp
ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA
Enzyme 12 GenBank Gene ID M22430 Link Image
Enzyme 12 GeneCard ID PLA2G2A Link Image
Enzyme 12 GenAtlas ID PLA2G2A Link Image
Enzyme 12 HGNC ID HGNC:9031 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 1p35
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Seilhamer JJ, Pruzanski W, Vadas P, Plant S, Miller JA, Kloss J, Johnson LK: Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid. J Biol Chem. 1989 Apr 5;264(10):5335-8. [PubMed Link Image]
  2. Kramer RM, Hession C, Johansen B, Hayes G, McGray P, Chow EP, Tizard R, Pepinsky RB: Structure and properties of a human non-pancreatic phospholipase A2. J Biol Chem. 1989 Apr 5;264(10):5768-75. [PubMed Link Image]
  3. Kramer RM, Johansen B, Hession C, Pepinsky RB: Structure and properties of a secretable phospholipase A2 from human platelets. Adv Exp Med Biol. 1990;275:35-53. [PubMed Link Image]
  4. Kanda A, Ono T, Yoshida N, Tojo H, Okamoto M: The primary structure of a membrane-associated phospholipase A2 from human spleen. Biochem Biophys Res Commun. 1989 Aug 30;163(1):42-8. [PubMed Link Image]
  5. Hara S, Kudo I, Matsuta K, Miyamoto T, Inoue K: Amino acid composition and NH2-terminal amino acid sequence of human phospholipase A2 purified from rheumatoid synovial fluid. J Biochem (Tokyo). 1988 Sep;104(3):326-8. [PubMed Link Image]
  6. Lai CY, Wada K: Phospholipase A2 from human synovial fluid: purification and structural homology to the placental enzyme. Biochem Biophys Res Commun. 1988 Dec 15;157(2):488-93. [PubMed Link Image]
  7. Minami T, Tojo H, Shinomura Y, Matsuzawa Y, Okamoto M: Purification and characterization of a phospholipase A2 from human ileal mucosa. Biochim Biophys Acta. 1993 Oct 13;1170(2):125-30. [PubMed Link Image]
  8. Wery JP, Schevitz RW, Clawson DK, Bobbitt JL, Dow ER, Gamboa G, Goodson T Jr, Hermann RB, Kramer RM, McClure DB, et al.: Structure of recombinant human rheumatoid arthritic synovial fluid phospholipase A2 at 2.2 A resolution. Nature. 1991 Jul 4;352(6330):79-82. [PubMed Link Image]
  9. Scott DL, White SP, Browning JL, Rosa JJ, Gelb MH, Sigler PB: Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate. Science. 1991 Nov 15;254(5034):1007-10. [PubMed Link Image]
  10. Schevitz RW, Bach NJ, Carlson DG, Chirgadze NY, Clawson DK, Dillard RD, Draheim SE, Hartley LW, Jones ND, Mihelich ED, et al.: Structure-based design of the first potent and selective inhibitor of human non-pancreatic secretory phospholipase A2. Nat Struct Biol. 1995 Jun;2(6):458-65. [PubMed Link Image]
  11. Kitadokoro K, Hagishita S, Sato T, Ohtani M, Miki K: Crystal structure of human secretory phospholipase A2-IIA complex with the potent indolizine inhibitor 120-1032. J Biochem (Tokyo). 1998 Apr;123(4):619-23. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5302
Enzyme 13 Name Group IID secretory phospholipase A2 precursor
Enzyme 13 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIID
  2. GIID sPLA2
  3. PLA2IID
  4. sPLA(2-IID
  5. Secretory-type PLA, stroma-associated homolog
Enzyme 13 Gene Name PLA2G2D
Enzyme 13 Protein Sequence >Group IID secretory phospholipase A2 precursor
MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDAT
DWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLK
RNLDTYQKRLRFYWRPHCRGQTPGC
Enzyme 13 Number of Residues 145
Enzyme 13 Molecular Weight 16546
Enzyme 13 Theoretical pI 8.28
Enzyme 13 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. L-alpha-1-palmitoyl-2- linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined
Enzyme 13 Pathways
Enzyme 13 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-20
Enzyme 13 Transmembrane Regions Not Available
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 5771420 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q9UNK4 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name PA2GD_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >438 bp
ATGGAACTTGCACTGCTGTGTGGGCTGGTGGTGATGGCTGGTGTGATTCCAATCCAGGGC
GGGATCCTGAACCTGAACAAGATGGTCAAGCAAGTGACTGGGAAAATGCCCATCCTCTCC
TACTGGCCCTACGGCTGTCACTGCGGACTAGGTGGCAGAGGCCAACCCAAAGATGCCACG
GACTGGTGCTGCCAGACCCATGACTGCTGCTATGACCACCTGAAGACCCAGGGGTGCGGC
ATCTACAAGGACTATTACAGATACAACTTTTCCCAGGGGAACATCCACTGCTCTGACAAG
GGAAGCTGGTGTGAGCAGCAGCTGTGTGCCTGTGACAAGGAGGTGGCCTTCTGCCTGAAG
CGCAACCTGGACACCTACCAGAAGCGACTGCGTTTCTACTGGCGGCCCCACTGCCGGGGG
CAGACCCCTGGGTGCTAG
Enzyme 13 GenBank Gene ID AF112982 Link Image
Enzyme 13 GeneCard ID PLA2G2D Link Image
Enzyme 13 GenAtlas ID PLA2G2D Link Image
Enzyme 13 HGNC ID HGNC:9033 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 1p36.12
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Ishizaki J, Suzuki N, Higashino K, Yokota Y, Ono T, Kawamoto K, Fujii N, Arita H, Hanasaki K: Cloning and characterization of novel mouse and human secretory phospholipase A(2)s. J Biol Chem. 1999 Aug 27;274(35):24973-9. [PubMed Link Image]
  2. Shakhov AN, Rubtsov AV, Lyakhov IG, Tumanov AV, Nedospasov SA: SPLASH (PLA2IID), a novel member of phospholipase A2 family, is associated with lymphotoxin deficiency. Genes Immun. 2000 Feb;1(3):191-9. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5453
Enzyme 14 Name Pancreatic triacylglycerol lipase precursor
Enzyme 14 Synonyms
  1. Pancreatic lipase
  2. PL
Enzyme 14 Gene Name PNLIP
Enzyme 14 Protein Sequence >Pancreatic triacylglycerol lipase precursor
MLPLWTLSLLLGAVAGKEVCYERLGCFSDDSPWSGITERPLHILPWSPKDVNTRFLLYTN
ENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGEENWLANVCKNLFKVESVNCIC
VDWKGGSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGR
RTNGTIGRITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDGAPIVPNLGFGMSQVVGH
LDFFPNGGVEMPGCKKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPDGFAGF
PCASYNVFTANKCFPCPSGGCPQMGHYADRYPGKTNDVGQKFYLDTGDASNFARWRYKVS
VTLSGKKVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWY
NNVINPTLPRVGASKIIVETNVGKQFNFCSPETVREEVLLTLTPC
Enzyme 14 Number of Residues 465
Enzyme 14 Molecular Weight 51157
Enzyme 14 Theoretical pI 6.72
Enzyme 14 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • triacylglycerol lipase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 14 Pathways
Enzyme 14 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-16
Enzyme 14 Transmembrane Regions Not Available
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 339597 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P16233 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name LIPP_HUMAN Link Image
Enzyme 14 PDB ID 1N8S Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1398 bp
ATGCTGCCACTTTGGACTCTTTCACTGCTGCTGGGAGCAGTAGCAGGAAAAGAAGTTTGC
TACGAAAGACTCGGCTGCTTCAGTGATGACTCCCCATGGTCAGGAATTACGGAAAGACCC
CTCCATATATTGCCTTGGTCTCCAAAAGATGTCAACACCCGCTTCCTCCTATATACTAAT
GAGAACCCAAACAACTTTCAAGAAGTTGCCGCAGATTCATCAAGCATCAGTGGCTCCAAT
TTCAAAACAAATAGAAAAACTCGCTTTATTATTCATGGATTCATAGACAAGGGAGAAGAA
AACTGGCTGGCCAATGTGTGCAAGAATCTGTTCAAGGTGGAAAGTGTGAACTGTATCTGT
GTGGACTGGAAAGGTGGCTCCCGAACTGGATACACACAAGCCTCGCAGAACATCAGGATC
GTGGGAGCAGAAGTGGCATATTTTGTTGAATTTCTTCAGTCGGCGTTCGGTTACTCACCT
TCCAACGTGCATGTCATTGGCCACAGCCTGGGTGCCCACGCTGCTGGGGAGGCTGGAAGG
AGAACCAATGGGACCATTGGACGCATCACAGGGTTGGACCCAGCAGAACCTTGCTTTCAG
GGCACACCTGAATTAGTCCGATTGGACCCCAGCGATGCCAAATTTGTGGATGTAATTCAC
ACGGATGGTGCCCCCATAGTCCCCAATTTGGGGTTTGGAATGAGCCAAGTCGTGGGCCAC
CTAGATTTCTTTCCAAATGGAGGAGTGGAAATGCCTGGATGTAAAAAGAACATTCTCTCT
CAGATTGTGGACATAGACGGAATCTGGGAAGGGACTCGAGACTTTGCGGCCTGTAATCAC
TTAAGAAGCTACAAATATTACACTGATAGCATCGTCAACCCTGATGGCTTTGCTGGATTC
CCCTGTGCCTCTTACAACGTCTTCACTGCAAACAAGTGTTTCCCTTGTCCAAGTGGAGGC
TGCCCACAGATGGGTCACTATGCTGATAGATATCCTGGGAAAACAAATGATGTGGGCCAG
AAATTTTATCTAGACACTGGTGATGCCAGTAATTTTGCACGTTGGAGGTATAAGGTATCT
GTCACACTGTCTGGAAAAAAGGTTACAGGACACATACTAGTTTCTTTGTTCGGAAATAAA
GGAAACTCTAAGCAGTATGAAATTTTCAAGGGCACTCTCAAACCAGATAGTACTCATTCC
AATGAATTTGACTCAGATGTGGATGTTGGGGACTTGCAGATGGTTAAATTTATTTGGTAT
AACAATGTGATCAACCCAACTTTACCTAGAGTGGGAGCATCCAAGATTATAGTGGAGACA
AATGTTGGAAAACAGTTCAACTTCTGTAGTCCAGAAACCGTCAGGGAGGAAGTTCTGCTC
ACCCTCACACCGTGTTAG
Enzyme 14 GenBank Gene ID J05125 Link Image
Enzyme 14 GeneCard ID PNLIP Link Image
Enzyme 14 GenAtlas ID PNLIP Link Image
Enzyme 14 HGNC ID HGNC:9155 Link Image
Enzyme 14 Chromosome Location 10
Enzyme 14 Locus 10q26.1
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Lowe ME, Rosenblum JL, Strauss AW: Cloning and characterization of human pancreatic lipase cDNA. J Biol Chem. 1989 Nov 25;264(33):20042-8. [PubMed Link Image]
  2. Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [PubMed Link Image]
  3. Sims HF, Jennens ML, Lowe ME: The human pancreatic lipase-encoding gene: structure and conservation of an Alu sequence in the lipase gene family. Gene. 1993 Sep 15;131(2):281-5. [PubMed Link Image]
  4. Winkler FK, D'Arcy A, Hunziker W: Structure of human pancreatic lipase. Nature. 1990 Feb 22;343(6260):771-4. [PubMed Link Image]
  5. van Tilbeurgh H, Sarda L, Verger R, Cambillau C: Structure of the pancreatic lipase-procolipase complex. Nature. 1992 Sep 10;359(6391):159-62. [PubMed Link Image]
  6. van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C: Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature. 1993 Apr 29;362(6423):814-20. [PubMed Link Image]
  7. Carriere F, Thirstrup K, Boel E, Verger R, Thim L: Structure-function relationships in naturally occurring mutants of pancreatic lipase. Protein Eng. 1994 Apr;7(4):563-9. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5458
Enzyme 15 Name Hepatic triacylglycerol lipase precursor
Enzyme 15 Synonyms
  1. Hepatic lipase
  2. HL
  3. Lipase member C
Enzyme 15 Gene Name LIPC
Enzyme 15 Protein Sequence >Hepatic triacylglycerol lipase precursor
MDTSPLCFSILLVLCIFIQSSALGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQ
GCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAALKSQPAQPVNVGLV
DWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSS
IGGTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGH
YDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAY
PCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKRLFLVTRAQSPFKVYHYQLKIQF
INQTETPIQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKW
ENSAVWANVWDTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQ
EKIFVKCEIKSKTSKRKIR
Enzyme 15 Number of Residues 499
Enzyme 15 Molecular Weight 55881
Enzyme 15 Theoretical pI 9.37
Enzyme 15 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • triacylglycerol lipase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin
Enzyme 15 Pathways
Enzyme 15 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-22
Enzyme 15 Transmembrane Regions Not Available
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 339595 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P11150 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name LIPC_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1500 bp
ATGGACACAAGTCCCCTGTGTTTCTCCATTCTGTTGGTTTTATGCATCTTTATCCAATCA
AGTGCCCTTGGACAAAGCCTGAAACCAGAGCCATTTGGAAGAAGAGCTCAAGCTGTTGAA
ACAAACAAAACGCTGCATGAGATGAAGACCAGATTCCTGCTCTTTGGAGAAACCAATCAG
GGCTGTCAGATTCGAATCAATCATCCGGACACGTTACAGGAGTGCGGCTTCAACTCCTCC
CTGCCTCTGGTGATGATAATCCACGGGTGGTCGGTGGACGGCGTGCTAGAAAACTGGATC
TGGCAGATGGTGGCCGCGCTGAAGTCTCAGCCGGCCCAGCCAGTGAACGTGGGGCTGGTG
GACTGGATCACCCTGGCCCACGACCACTACACCATCGCCGTCCGCAACACCCGCCTTGTG
GGCAAGGAGGTCGCGGCTCTTCTCCGGTGGCTGGAGGAATCTGTGCAACTCTCTCGAAGC
CATGTTCACCTAATTGGGTACAGCCTGGGTGCACACGTGTCAGGATTTGCCGGCAGTTCC
ATCGGTGGAACGCACAAGATTGGGAGAATCACAGGGCTGGATGCCGCGGGACCTTTGTTT
GAGGGAAGTGCCCCCAGCAATCGTCTTTCTCCAGATGATGCCAATTTTGTGGATGCCATT
CATACCTTTACGCGGGAGCACATGGGCCTGAGCGTGGGCATCAAACAGCCCATAGGACAC
TATGACTTCTATCCCAACGGGGGCTCCTTCCAGCCTGGCTGCCACTCCCTAGAGCTCTAC
AGACATATTGCCCAGCACGGCTTCAATGCCATCACCCAGACCATAAAATGCTCCCACGAG
CGATCGGTGCACCTTTTCATCGACTCCTTGCTGCACGCCGGCACGCAGAGCATGGCCTAC
CCGTGTGGTGACATGAACAGCTTCAGCCAGGGCCTGTGCCTGAGCTGCAAGAAGGGCCGC
TGCAACACGCTGGGCTACCACGTCCGCCAGGAGCCGCGGAGCAAGAGCAAGAGGCTCTTC
CTCGTAACGCGAGCCCAGTCCCCCTTCAAAGTTTATCATTACCAGTTAAAGATCCAGTTC
ATCAACCAAACTGAGACGCCAATACAAACAACTTTTACCATGTCACTACTCGGAACAAAA
GAGAAAATGCAGAAAATTCCCATCACTCTGGGCAAAGGAATTGCTAGTAATAAAACGTAT
TCCTTTCTTATCACGCTGGATGTGGATATCGGCGAGCTGATCATGATCAAGTTCAAGTGG
GAAAACAGTGCAGTGTGGGCCAATGTCTGGGACACGGTCCAGACCATCATCCCATGGAGC
ACAGGGCCGCGCCACTCAGGCCTCGTTCTGAAGACGATCAGAGTCAAAGCAGGAGAAACC
CAGCAAAGAATGACATTTTGTTCAGAAAACACAGATGACCTACTACTTCGCCCAACCCAG
GAAAAAATCTTCGTGAAATGTGAAATAAAGTCTAAAACATCAAAGCGAAAGATCAGATGA
Enzyme 15 GenBank Gene ID J03895 Link Image
Enzyme 15 GeneCard ID LIPC Link Image
Enzyme 15 GenAtlas ID LIPC Link Image
Enzyme 15 HGNC ID HGNC:6619 Link Image
Enzyme 15 Chromosome Location 15
Enzyme 15 Locus 15q21-q23
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Martin GA, Busch SJ, Meredith GD, Cardin AD, Blankenship DT, Mao SJ, Rechtin AE, Woods CW, Racke MM, Schafer MP, et al.: Isolation and cDNA sequence of human postheparin plasma hepatic triglyceride lipase. J Biol Chem. 1988 Aug 5;263(22):10907-14. [PubMed Link Image]
  2. Stahnke G, Sprengel R, Augustin J, Will H: Human hepatic triglyceride lipase: cDNA cloning, amino acid sequence and expression in a cultured cell line. Differentiation. 1987;35(1):45-52. [PubMed Link Image]
  3. Datta S, Luo CC, Li WH, VanTuinen P, Ledbetter DH, Brown MA, Chen SH, Liu SW, Chan L: Human hepatic lipase. Cloned cDNA sequence, restriction fragment length polymorphisms, chromosomal localization, and evolutionary relationships with lipoprotein lipase and pancreatic lipase. J Biol Chem. 1988 Jan 25;263(3):1107-10. [PubMed Link Image]
  4. Cai SJ, Wong DM, Chen SH, Chan L: Structure of the human hepatic triglyceride lipase gene. Biochemistry. 1989 Nov 14;28(23):8966-71. [PubMed Link Image]
  5. Ameis D, Stahnke G, Kobayashi J, McLean J, Lee G, Buscher M, Schotz MC, Will H: Isolation and characterization of the human hepatic lipase gene. J Biol Chem. 1990 Apr 25;265(12):6552-5. [PubMed Link Image]
  6. Takagi A, Ikeda Y, Mori A, Ashida Y, Yamamoto A: Identification of a BstNI polymorphism in exon 9 of the human hepatic triglyceride lipase gene. Mol Cell Probes. 1996 Aug;10(4):313-4. [PubMed Link Image]
  7. Hegele RA, Tu L, Connelly PW: Human hepatic lipase mutations and polymorphisms. Hum Mutat. 1992;1(4):320-4. [PubMed Link Image]
  8. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  9. Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5461
Enzyme 16 Name Pancreatic lipase-related protein 1 precursor
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name PNLIPRP1
Enzyme 16 Protein Sequence >Pancreatic lipase-related protein 1 precursor
MLIFWTITLFLLGAAKGKEVCYEDLGCFSDTEPWGGTAIRPLKILPWSPEKIGTRFLLYT
NENPNNFQILLLSDPSTIEASNFQMDRKTRFIIHGFIDKGDESWVTDMCKKLFEVEEVNC
ICVDWKKGSQATYTQAANNVRVVGAQVAQMLDILLTEYSYPPSKVHLIGHSLGAHVAGEA
GSKTPGLSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPLIPFLGFGTNQQMG
HLDFFPNGGESMPGCKKNALSQIVDLDGIWAGTRDFVACNHLRSYKYYLESILNPDGFAA
YPCTSYKSFESDKCFPCPDQGCPQMGHYADKFAGRTSEEQQKFFLNTGEASNFARWRYGV
SITLSGRTATGQIKVALFGNKGNTHQYSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLW
NNNVINPTLPKVGATKITVQKGEEKTVYNFCSEDTVREDTLLTLTPC
Enzyme 16 Number of Residues 467
Enzyme 16 Molecular Weight 51848
Enzyme 16 Theoretical pI 5.47
Enzyme 16 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • triacylglycerol lipase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 16 Pathways
Enzyme 16 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-17
Enzyme 16 Transmembrane Regions Not Available
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 187230 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P54315 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name LIPR1_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1404 bp
ATGCTGATCTTCTGGACAATCACACTTTTCCTGCTGGGAGCAGCCAAAGGAAAAGAAGTT
TGCTATGAGGACCTCGGGTGCTTTTCTGACACTGAGCCCTGGGGCGGGACAGCAATCAGG
CCCCTGAAAATTCTCCCCTGGAGCCCTGAGAAGATCGGCACCCGCTTCCTGCTGTACACC
AATGAAAACCCAAACAACTTTCAAATTCTCCTCCTCTCTGATCCATCAACAATTGAGGCA
TCAAATTTTCAAATGGACAGAAAGACCCGGTTCATCATCCATGGCTTCATAGACAAAGGA
GATGAGAGCTGGGTGACAGACATGTGCAAGAAACTGTTCGAGGTGGAGGAGGTGAACTGC
ATCTGCGTGGACTGGAAGAAGGGCTCCCAAGCCACCTACACACAGGCTGCCAACAACGTG
CGAGTGGTGGGCGCCCAGGTGGCCCAGATGCTCGACATCCTCTTGACAGAGTATAGCTAC
CCCCCTTCCAAAGTTCACCTCATTGGCCACAGCCTGGGAGCCCACGTGGCTGGAGAGGCA
GGAAGCAAGACTCCAGGCCTGAGCAGGATTACAGGGTTGGATCCTGTAGAAGCAAGTTTC
GAGAGTACTCCTGAAGAGGTGCGACTTGATCCCTCTGATGCTGACTTTGTTGATGTGATT
CACACGGATGCAGCTCCCCTGATCCCATTCTTGGGTTTTGGAACGAACCAACAGATGGGT
CATCTTGACTTCTTCCCCAATGGAGGAGAGAGCATGCCGGGATGCAAGAAGAATGCCCTG
TCTCAGATCGTGGATCTAGATGGCATCTGGGCGGGAACCCGGGACTTTGTGGCTTGCAAT
CACCTAAGAAGCTACAAGTATTACTTGGAAAGCATCCTCAATCCCGATGGGTTTGCTGCA
TATCCCTGCACTTCCTACAAGTCCTTTGAGTCTGACAAGTGCTTCCCGTGTCCAGATCAA
GGATGCCCACAGATGGGTCACTATGCTGATAAATTTGCTGGCAGGACAAGTGAAGAGCAG
CAGAAATTCTTCTTGAACACAGGAGAGGCTAGCAATTTCGCTCGCTGGAGATATGGGGTT
TCCATCACACTGTCTGGAAGAACAGCCACTGGTCAGATCAAAGTTGCTTTGTTTGGAAAT
AAGGGAAACACTCACCAGTACAGCATCTTCAGGGGGATTCTCAAACCAGGCTCAACCCAT
TCCTATGAGTTTGATGCAAAGCTGGATGTTGGAACAATTGAGAAAGTCAAGTTTCTTTGG
AATAACAATGTGATAAATCCAACCCTCCCCAAAGTGGGTGCCACCAAGATCACTGTGCAA
AAGGGAGAAGAGAAGACAGTGTACAACTTCTGTAGCGAAGACACAGTGCGGGAAGACACG
CTGCTCACCCTCACGCCCTGCTAA
Enzyme 16 GenBank Gene ID M93283 Link Image
Enzyme 16 GeneCard ID PNLIPRP1 Link Image
Enzyme 16 GenAtlas ID PNLIPRP1 Link Image
Enzyme 16 HGNC ID HGNC:9156 Link Image
Enzyme 16 Chromosome Location 10
Enzyme 16 Locus 10q25.3
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5464
Enzyme 17 Name Adiponutrin
Enzyme 17 Synonyms
  1. iPLA2-epsilon
  2. Calcium-independent phospholipase A2- epsilon
  3. Patatin-like phospholipase domain-containing protein 3[Includes: Triacylglycerol lipase
Enzyme 17 Gene Name PNPLA3
Enzyme 17 Protein Sequence >Adiponutrin
MYDAERGWSLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGI
PLEQTLQVLSDLVRKARSRNIGIFHPSFNLSKFLRQGLCKCLPANVHQLISGKIGISLTR
VSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDGGVSDNVPFIDAKT
TITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLR
GYLDAFRFLEEKGICNRPQPGLKSSSEGMDPEVAMPSWANMSLDSSPESAALAVRLEGDE
LLDHLRLSILPWDESILDTLSPRLATALSEEMKDKGGYMSKICNLLPIRIMSYVMLPCTL
PVESAIAIVQRLVTWLPDMPDDVLWLQWVTSQVFTRVLMCLLPASRSQMPVSSQQASPCT
PEQDWPCWTPCSPKGCPAETKAEATPRSILRSSLNFFLGNKVPAGAEGLSTFPSFSLEKS
L
Enzyme 17 Number of Residues 481
Enzyme 17 Molecular Weight 52866
Enzyme 17 Theoretical pI 6.68
Enzyme 17 GO Classification Not Available
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Multifunctional enzyme which has both triacylglycerol lipase and acylglycerol O-acyltransferase activities
Enzyme 17 Pathways
Enzyme 17 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate
Enzyme 17 Pfam Domain Function Not Available
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • 42-62
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 17059636 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q9NST1 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name ADPN_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1446 bp
ATGTACGACGCAGAGCGCGGCTGGAGCTTGTCCTTCGCGGGCTGCGGCTTCCTGGGCTTC
TACCACGTCGGGGCGACCCGCTGCCTGAGCGAGCACGCCCCGCACCTCCTCCGCGACGCG
CGCATGTTGTTCGGCGCTTCGGCCGGGGCGTTGCACTGCGTCGGCGTCCTCTCCGGTATC
CCGCTGGAGCAGACTCTGCAGGTCCTCTCAGATCTTGTGCGGAAGGCCAGGAGTCGGAAC
ATTGGCATCTTCCATCCATCCTTCAACTTAAGCAAGTTCCTCCGACAGGGTCTCTGCAAA
TGCCTCCCGGCCAATGTCCACCAGCTCATCTCCGGCAAAATAGGCATCTCTCTTACCAGA
GTGTCTGATGGGGAAAACGTTCTGGTGTCTGACTTTCGGTCCAAAGACGAAGTCGTGGAT
GCCTTGGTATGTTCCTGCTTCATCCCCTTCTACAGTGGCCTTATCCCTCCTTCCTTCAGA
GGCGTGCGATATGTGGATGGAGGAGTGAGTGACAACGTACCCTTCATTGATGCCAAAACA
ACCATCACCGTGTCCCCCTTCTATGGGGAGTACGACATCTGCCCTAAAGTCAAGTCCACG
AACTTTCTTCATGTGGACATCACCAAGCTCAGTCTACGCCTCTGCACAGGGAACCTCTAC
CTTCTCTCGAGAGCTTTTGTCCCCCCGGATCTCAAGGTGCTGGGAGAGATATGCCTTCGA
GGATATTTGGATGCATTCAGGTTCTTGGAAGAGAAGGGCATCTGCAACAGGCCCCAGCCA
GGCCTGAAGTCATCCTCAGAAGGGATGGATCCTGAGGTCGCCATGCCCAGCTGGGCAAAC
ATGAGTCTGGATTCTTCCCCGGAGTCGGCTGCCTTGGCTGTGAGGCTGGAGGGAGATGAG
CTGCTAGACCACCTGCGTCTCAGCATCCTGCCCTGGGATGAGAGCATCCTGGACACCCTC
TCGCCCAGGCTCGCTACAGCACTGAGTGAAGAAATGAAAGACAAAGGTGGATACATGAGC
AAGATTTGCAACTTGCTACCCATTAGGATAATGTCTTATGTAATGCTGCCCTGTACCCTG
CCTGTGGAATCTGCCATTGCGATTGTCCAGAGACTGGTGACATGGCTTCCAGATATGCCC
GACGATGTCCTGTGGTTGCAGTGGGTGACCTCACAGGTGTTCACTCGAGTGCTGATGTGT
CTGCTCCCCGCCTCCAGGTCCCAAATGCCAGTGAGCAGCCAACAGGCCTCCCCATGCACA
CCTGAGCAGGACTGGCCCTGCTGGACTCCCTGCTCCCCCAAGGGCTGTCCAGCAGAGACC
AAAGCAGAGGCCACCCCGCGGTCCATCCTCAGGTCCAGCCTGAACTTCTTCTTGGGCAAT
AAAGTACCTGCTGGTGCTGAGGGGCTCTCCACCTTTCCCAGTTTTTCACTAGAGAAGAGT
CTGTGA
Enzyme 17 GenBank Gene ID AL138578 Link Image
Enzyme 17 GeneCard ID PNPLA3 Link Image
Enzyme 17 GenAtlas ID PNPLA3 Link Image
Enzyme 17 HGNC ID HGNC:18590 Link Image
Enzyme 17 Chromosome Location 22
Enzyme 17 Locus 22q13.31
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5468
Enzyme 18 Name Gastric triacylglycerol lipase precursor
Enzyme 18 Synonyms
  1. Gastric lipase
  2. GL
Enzyme 18 Gene Name LIPF
Enzyme 18 Protein Sequence >Gastric triacylglycerol lipase precursor
MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILE
VNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRG
NTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFI
AFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQF
LATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKS
GKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPN
LIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK
Enzyme 18 Number of Residues 398
Enzyme 18 Molecular Weight 45238
Enzyme 18 Theoretical pI 7.37
Enzyme 18 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 18 Pathways
Enzyme 18 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-19
Enzyme 18 Transmembrane Regions Not Available
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 758063 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P07098 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name LIPG_HUMAN Link Image
Enzyme 18 PDB ID 1HLG Link Image
Enzyme 18 PDB File Show
Enzyme 18 3D Structure
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1197 bp
ATGTGGCTGCTTTTAACAATGGCAAGTTTGATATCTGTACTGGGGACTACACATGGTTTG
TTTGGAAAATTACATCCTGGAAGCCCTGAAGTGACTATGAACATTAGTCAGATGATTACT
TATTGGGGATACCCAAATGAAGAATATGAAGTTGTGACTGAAGATGGTTATATTCTTGAA
GTCAATAGAATTCCTTATGGGAAGAAAAATTCAGGGAATACAGGCCAGAGACCTGTTGTG
TTTTTGCAGCATGGTTTGCTTGCATCAGCCACAAACTGGATTTCCAACCTGCCGAACAAC
AGCCTTGCCTTCATTCTGGCAGATGCTGGTTATGATGTGTGGCTGGGCAACAGCAGAGGA
AACACCTGGGCCAGAAGAAACTTGTACTATTCACCAGATTCAGTTGAATTCTGGGCTTTC
AGCTTTGATGAAATGGCTAAATATGACCTTCCAGCCACAATCGACTTCATTGTAAAGAAA
ACTGGACAGAAGCAGCTACACTATGTTGGCCATTCCCAGGGCACCACCATTGGTTTTATT
GCCTTTTCCACCAATCCCAGCCTGGCTAAAAGAATCAAAACCTTCTATGCTCTAGCTCCT
GTTGCCACTGTGAAGTATACAAAAAGCCTTATAAACAAACTTAGATTTGTTCCTCAATCC
CTCTTCAAGTTTATATTTGGTGACAAAATATTCTACCCACACAACTTCTTTGATCAATTT
CTTGCTACTGAAGTGTGCTCCCGTGAGATGCTGAATCTCCTTTGCAGCAATGCCTTATTT
ATAATTTGTGGATTTGACAGTAAGAACTTTAACACGAGTCGCTTGGATGTGTATCTATCA
CATAATCCAGCAGGAACTTCTGTTCAAAACATGTTCCATTGGACCCAGGCTGTTAAGTCT
GGGAAATTCCAAGCTTATGACTGGGGAAGCCCAGTTCAGAATAGGATGCACTATGATCAG
TCCCAACCTCCCTACTACAATGTGACAGCCATGAATGTACCAATTGCAGTGTGGAACGGT
GGCAAGGACCTGTTGGCTGACCCCCAAGATGTTGGCCTTTTGCTTCCAAAACTCCCCAAT
CTTATTTACCACAAGGAGATTCCTTTTTACAATCACTTGGACTTTATCTGGGCAATGGAT
GCCCCTCAAGAAGTTTACAATGACATTGTTTCTATGATATCAGAAGATAAAAAGTAG
Enzyme 18 GenBank Gene ID X05997 Link Image
Enzyme 18 GeneCard ID LIPF Link Image
Enzyme 18 GenAtlas ID LIPF Link Image
Enzyme 18 HGNC ID HGNC:6622 Link Image
Enzyme 18 Chromosome Location 10
Enzyme 18 Locus 10q23.31
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Bodmer MW, Angal S, Yarranton GT, Harris TJ, Lyons A, King DJ, Pieroni G, Riviere C, Verger R, Lowe PA: Molecular cloning of a human gastric lipase and expression of the enzyme in yeast. Biochim Biophys Acta. 1987 Aug 25;909(3):237-44. [PubMed Link Image]
  2. Bernback S, Blackberg L: Human gastric lipase. The N-terminal tetrapeptide is essential for lipid binding and lipase activity. Eur J Biochem. 1989 Jul 1;182(3):495-9. [PubMed Link Image]
  3. Roussel A, Canaan S, Egloff MP, Riviere M, Dupuis L, Verger R, Cambillau C: Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest. J Biol Chem. 1999 Jun 11;274(24):16995-7002. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5471
Enzyme 19 Name Endothelial lipase precursor
Enzyme 19 Synonyms
  1. Endothelial cell-derived lipase
  2. EDL
  3. EL
Enzyme 19 Gene Name LIPG
Enzyme 19 Protein Sequence >Endothelial lipase precursor
MSNSVPLLCFWSLCYCFAAGSPVPFGPEGRLEDKLHKPKATQTEVKPSVRFNLRTSKDPE
HEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVV
VDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGN
FVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTRSFGLSIGIQMPVGHID
IYPNGGDFQPGCGLNDVLGSIAYGTITEVVKCEHERAVHLFVDSLVNQDKPSFAFQCTDS
NRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKN
MGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGAS
QSWYNLWKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWF
RKCRDGWRMKNETSPTVELP
Enzyme 19 Number of Residues 500
Enzyme 19 Molecular Weight 56795
Enzyme 19 Theoretical pI 8.00
Enzyme 19 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • lipoprotein lipase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin
Enzyme 19 Pathways
Enzyme 19 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-20
Enzyme 19 Transmembrane Regions Not Available
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 4836419 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9Y5X9 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name LIPE_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1503 bp
ATGAGCAACTCCGTTCCTCTGCTCTGTTTCTGGAGCCTCTGCTATTGCTTTGCTGCGGGG
AGCCCCGTACCTTTTGGTCCAGAGGGACGGCTGGAAGATAAGCTCCACAAACCCAAAGCT
ACACAGACTGAGGTCAAACCATCTGTGAGGTTTAACCTCCGCACCTCCAAGGACCCAGAG
CATGAAGGATGCTACCTCTCCGTCGGCCACAGCCAGCCCTTAGAAGACTGCAGTTTCAAC
ATGACAGCTAAAACCTTTTTCATCATTCACGGATGGACGATGAGCGGTATCTTTGAAAAC
TGGCTGCACAAACTCGTGTCAGCCCTGCACACAAGAGAGAAAGACGCCAATGTAGTTGTG
GTTGACTGGCTCCCCCTGGCCCACCAGCTTTACACGGATGCGGTCAATAATACCAGGGTG
GTGGGACACAGCATTGCCAGGATGCTCGACTGGCTGCAGGAGAAGGACGATTTTTCTCTC
GGGAATGTCCACTTGATCGGCTACAGCCTCGGAGCGCACGTGGCCGGGTATGCAGGCAAC
TTCGTGAAAGGAACGGTGGGCCGAATCACAGGTTTGGATCCTGCCGGGCCCATGTTTGAA
GGGGCCGACATCCACAAGAGGCTCTCTCCGGACGATGCAGATTTTGTGGATGTCCTCCAC
ACCTACACGCGTTCCTTCGGCTTGAGCATTGGTATTCAGATGCCTGTGGGCCACATTGAC
ATCTACCCCAATGGGGGTGACTTCCAGCCAGGCTGTGGACTCAACGATGTCTTGGGATCA
ATTGCATATGGAACAATCACAGAGGTGGTAAAATGTGAGCATGAGCGAGCCGTCCACCTC
TTTGTTGACTCTCTGGTGAATCAGGACAAGCCGAGTTTTGCCTTCCAGTGCACTGACTCC
AATCGCTTCAAAAAGGGGATCTGTCTGAGCTGCCGCAAGAACCGTTGTAATAGCATTGGC
TACAATGCCAAGAAAATGAGGAACAAGAGGAACAGCAAAATGTACCTAAAAACCCGGGCA
GGCATGCCTTTCAGAGTTTACCATTATCAGATGAAAATCCATGTCTTCAGTTACAAGAAC
ATGGGAGAAATTGAGCCCACCTTTTACGTCACCCTTTATGGCACTAATGCAGATTCCCAG
ACTCTGCCACTGGAAATAGTGGAGCGGATCGAGCAGAATGCCACCAACACCTTCCTGGTC
TACACCGAGGAGGACTTGGGAGACCTCTTGAAGATCCAGCTCACCTGGGAGGGGGCCTCT
CAGTCTTGGTACAACCTGTGGAAGGAGTTTCGCAGCTACCTGTCTCAACCCCGCAACCCC
GGACGGGAGCTGAATATCAGGCGCATCCGGGTGAAGTCTGGGGAAACCCAGCGGAAACTG
ACATTTTGTACAGAAGACCCTGAGAACACCAGCATATCCCCAGGCCGGGAGCTCTGGTTT
CGCAAGTGTCGGGATGGCTGGAGGATGAAAAACGAAACCAGTCCCACTGTGGAGCTTCCC
TGA
Enzyme 19 GenBank Gene ID AF118767 Link Image
Enzyme 19 GeneCard ID LIPG Link Image
Enzyme 19 GenAtlas ID LIPG Link Image
Enzyme 19 HGNC ID HGNC:6623 Link Image
Enzyme 19 Chromosome Location 18
Enzyme 19 Locus 18q21.1
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Hirata K, Dichek HL, Cioffi JA, Choi SY, Leeper NJ, Quintana L, Kronmal GS, Cooper AD, Quertermous T: Cloning of a unique lipase from endothelial cells extends the lipase gene family. J Biol Chem. 1999 May 14;274(20):14170-5. [PubMed Link Image]
  2. Jaye M, Lynch KJ, Krawiec J, Marchadier D, Maugeais C, Doan K, South V, Amin D, Perrone M, Rader DJ: A novel endothelial-derived lipase that modulates HDL metabolism. Nat Genet. 1999 Apr;21(4):424-8. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. McCoy MG, Sun GS, Marchadier D, Maugeais C, Glick JM, Rader DJ: Characterization of the lipolytic activity of endothelial lipase. J Lipid Res. 2002 Jun;43(6):921-9. [PubMed Link Image]
  5. Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5473
Enzyme 20 Name Bile salt-activated lipase precursor
Enzyme 20 Synonyms
  1. BAL
  2. Bile salt-stimulated lipase
  3. BSSL
  4. Carboxyl ester lipase
  5. Sterol esterase
  6. Cholesterol esterase
  7. Pancreatic lysophospholipase
Enzyme 20 Gene Name CEL
Enzyme 20 Protein Sequence >Bile salt-activated lipase precursor
MGRLQLVVLGLTCCWAVASAAKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTK
ALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLPV
MIWIYGGAFLMGSGHGANFLNNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPG
NYGLRDQHMAIAWVKRNIAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQS
GVALSPWVIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGLEYP
MLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASIDMPAINKGNKKVT
EEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQENKKKTVVDFETDVLFLVPTEIA
LAQHRANAKSAKTYAYLFSHPSRMPVYPKWVGADHADDIQYVFGKPFATPTGYRPQDRTV
SKAMIAYWTNFAKTGDPNMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLR
YWTLTYLALPTVTDQEATPVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSG
APPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVP
PTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDSGAPPVPPTGDS
EAAPVPPTDDSKEAQMPAVIRF
Enzyme 20 Number of Residues 742
Enzyme 20 Molecular Weight 78346
Enzyme 20 Theoretical pI 5.01
Enzyme 20 GO Classification Not Available
Enzyme 20 General Function Lipid transport and metabolism
Enzyme 20 Specific Function Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides
Enzyme 20 Pathways
Enzyme 20 Reactions
  • A steryl ester + H2O = a sterol + a fatty acid
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • 1-20
Enzyme 20 Transmembrane Regions Not Available
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 29501 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P19835 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name CEL_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >2238 bp
ATGCTCACCATGGGGCGCCTGCAACTGGTTGTGTTGGGCCTCACCTGCTGCTGGGCAGTG
GCGAGTGCCGCGAAGCTGGGCGCCGTGTACACAGAAGGTGGGTTCGTGGAAGGCGTCAAT
AAGAAGCTCGGCCTCCTGGGTGACTCTGTGGACATCTTCAAGGGCATCCCCTTCGCAGCT
CCCACCAAGGCCCTGGAAAATCCTCAGCCACATCCTGGCTGGCAAGGGACCCTGAAGGCC
AAGAACTTCAAGAAGAGATGCCTGCAGGCCACCATCACCCAGGACAGCACCTACGGGGAT
GAAGACTGCCTGTACCTCAACATTTGGGTGCCCCAGGGCAGGAAGCAAGTCTCCCGGGAC
CTGCCCGTTATGATCTGGATCTATGGAGGCGCCTTCCTCATGGGGTCCGGCCATGGGGCC
AACTTCCTCAACAACTACCTGTATGACGGCGAGGAGATCGCCACACGCGGAAACGTCATC
GTGGTCACCTTCAACTACCGTGTCGGCCCCCTTGGGTTCCTCAGCACTGGGGACGCCAAT
CTGCCAGGTAACTATGGCCTTCGGGATCAGCACATGGCCATTGCTTGGGTGAAGAGGAAT
ATCGCGGCCTTCGGGGGGGACCCCAACAACATCACGCTCTTCGGGGAGTCTGCTGGAGGT
GCCAGCGTCTCTCTGCAGACCCTCTCCCCCTACAACAAGGGCCTCATCCGGCGAGCCATC
AGCCAGAGCGGCGTGGCCCTGAGTCCCTGGGTCATCCAGAAAAACCCACTCTTCTGGGCC
AAAAAGGTGGCTGAGAAGGTGGGTTGCCCTGTGGGTGATGCCGCCAGGATGGCCCAGTGT
CTGAAGGTTACTGATCCCCGAGCCCTGACGCTGGCCTATAAGGTGCCGCTGGCAGGCCTG
GAGTACCCCATGCTGCACTATGTGGGCTTCGTCCCTGTCATTGATGGAGACTTCATCCCC
GCTGACCCGATCAACCTGTACGCCAACGCCGCCGACATCGACTATATAGCAGGCACCAAC
AACATGGACGGCCACATCTTCGCCAGCATCGACATGCCTGCCATCAACAAGGGCAACAAG
AAAGTCACGGAGGAGGACTTCTACAAGCTGGTCAGTGAGTTCACAATCACCAAGGGGCTC
AGAGGCGCCAAGACGACCTTTGATGTCTACACCGAGTCCTGGGCCCAGGACCCATCCCAG
GAGAATAAGAAGAAGACTGTGGTGGACTTTGAGACCGATGTCCTCTTCCTGGTGCCCACC
GAGATTGCCCTAGCCCAGCACAGAGCCAATGCCAAGAGTGCCAAGACCTACGCCTACCTG
TTTTCCCATCCCTCTCGGATGCCCGTCTACCCCAAATGGGTGGGGGCCGACCATGCAGAT
GACATTCAGTACGTTTTCGGGAAGCCCTTCGCCACCCCCACGGGCTACCGGCCCCAAGAC
AGGACAGTCTCTAAGGCCATGATCGCCTACTGGACCAACTTTGCCAAAACAGGGGACCCC
AACATGGGCGACTCGGCTGTGCCCACACACTGGGAACCCTACACTACGGAAAACAGCGGC
TACCTGGAGATCACCAAGAAGATGGGCAGCAGCTCCATGAAGCGGAGCCTGAGAACCAAC
TTCCTGCGCTACTGGACCCTCACCTATCTGGCGCTGCCCACAGTGACCGACCAGGAGGCC
ACCCCTGTGCCCCCCACAGGGGACTCCGAGGCCACTCCCGTGCCCCCCACGGGTGACTCC
GAGACCGCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGT
GACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCC
ACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTG
CCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGCGCCCCC
CCCGTGCCGCCCACGGGTGACGCCGGGCCCCCCCCCGTGCCGCCCACGGGTGACTCCGGC
GCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGACCCCCACGGGTGAC
TCCGAGACCGCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCTGTGCCCCCCACG
GGTGACTCTGAGGCTGCCCCTGTGCCCCCCACAGATGACTCCAAGGAAGCTCAGATGCCT
GCAGTCATTAGGTTTTAG
Enzyme 20 GenBank Gene ID X54457 Link Image
Enzyme 20 GeneCard ID CEL Link Image
Enzyme 20 GenAtlas ID CEL Link Image
Enzyme 20 HGNC ID HGNC:1848 Link Image
Enzyme 20 Chromosome Location 9
Enzyme 20 Locus 9q34.3
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Nilsson J, Blackberg L, Carlsson P, Enerback S, Hernell O, Bjursell G: cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase. Eur J Biochem. 1990 Sep 11;192(2):543-50. [PubMed Link Image]
  2. Hui DY, Kissel JA: Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase. FEBS Lett. 1990 Dec 10;276(1-2):131-4. [PubMed Link Image]
  3. Baba T, Downs D, Jackson KW, Tang J, Wang CS: Structure of human milk bile salt activated lipase. Biochemistry. 1991 Jan 15;30(2):500-10. [PubMed Link Image]
  4. Lidberg U, Nilsson J, Stromberg K, Stenman G, Sahlin P, Enerback S, Bjursell G: Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene. Genomics. 1992 Jul;13(3):630-40. [PubMed Link Image]
  5. Roudani S, Miralles F, Margotat A, Escribano MJ, Lombardo D: Bile salt-dependent lipase transcripts in human fetal tissues. Biochim Biophys Acta. 1995 Oct 17;1264(1):141-50. [PubMed Link Image]
  6. Christie DL, Cleverly DR, O'Connor CJ: Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases. FEBS Lett. 1991 Jan 28;278(2):190-4. [PubMed Link Image]
  7. Wang CS, Dashti A, Jackson KW, Yeh JC, Cummings RD, Tang J: Isolation and characterization of human milk bile salt-activated lipase C-tail fragment. Biochemistry. 1995 Aug 22;34(33):10639-44. [PubMed Link Image]
  8. Mechref Y, Chen P, Novotny MV: Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk. Glycobiology. 1999 Mar;9(3):227-34. [PubMed Link Image]
  9. Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC: Crystal structure of the catalytic domain of human bile salt activated lipase. Protein Sci. 2000 Sep;9(9):1783-90. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5477
Enzyme 21 Name Pancreatic lipase-related protein 2 precursor
Enzyme 21 Synonyms Not Available
Enzyme 21 Gene Name PNLIPRP2
Enzyme 21 Protein Sequence >Pancreatic lipase-related protein 2 precursor
MLPPWTLGLLLLATVRGKEVCYGQLGCFSDEKPWAGTLQRPVKLLPWSPEDIDTRFLLYT
NENPNNFQLITGTEPDTIEASNFQLDRKTRFIIHGFLDKAEDSWPSDMCKKMFEVEKVNC
ICVDWRHGSRAMYTQAVQNIRVVGAETAFLIQALSTQLGYSLEDVHVIGHSLGAHTAAEA
GRRLGGRVGRITGLDPAGPCFQDEPEEVRLDPSDAVFVDVIHTDSSPIVPSLGFGMSQKV
GHLDFFPNGGKEMPGCKKNVLSTITDIDGIWEGIGGFVSCNHLRSFEYYSSSVLNPDGFL
GYPCASYDEFQESKCFPCPAEGCPKMGHYADQFKGKTSAVEQTFFLNTGESGNFTSWRYK
VSVTLSGKEKVNGYIRIALYGSNENSKQYEIFKGSLKPDASHTCAIDVDFNVGKIQKVKF
LWNKRGINLSEPKLGASQITVQSGEDGTEYNFCSSDTVEENVLQSLYPC
Enzyme 21 Number of Residues 469
Enzyme 21 Molecular Weight 51947
Enzyme 21 Theoretical pI 5.11
Enzyme 21 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • triacylglycerol lipase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 21 Pathways
Enzyme 21 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • 1-17
Enzyme 21 Transmembrane Regions Not Available
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 187232 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID P54317 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name LIPR2_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1410 bp
ATGCTGCCCCCTTGGACCCTCGGCCTTCTCCTGCTGGCCACAGTCAGAGGAAAAGAGGTC
TGCTACGGACAACTTGGCTGCTTTTCTGATGAAAAACCATGGGCAGGAACCCTTCAGCGA
CCTGTAAAATTACTTCCCTGGTCCCCCGAGGACATTGACACCCGCTTTCTTCTGTACACA
AATGAAAATCCAAACAACTTCCAACTAATCACTGGCACGGAACCAGACACCATTGAGGCT
TCAAACTTCCAACTGGACCGCAAGACACGCTTCATCATCCATGGCTTCTTAGACAAGGCG
GAGGACAGCTGGCCATCGGACATGTGCAAGAAAATGTTTGAAGTGGAGAAGGTGAACTGC
ATCTGTGTGGACTGGAGGCACGGGTCCCGGGCAATGTACACCCAAGCCGTGCAAAACATT
CGGGTTGTTGGGGCGGAGACAGCTTTCTTAATACAAGCACTGTCGACGCAGCTAGGGTAC
AGCCTTGAGGACGTGCATGTCATCGGCCACAGCCTGGGCGCGCACACGGCCGCGGAGGCG
GGCAGGAGGCTGGGGGGCCGCGTGGGCAGGATCACAGGGCTGGATCCAGCAGGGCCGTGC
TTCCAGGATGAACCTGAGGAGGTTCGGTTGGATCCATCTGACGCCGTGTTTGTGGATGTG
ATTCACACAGATTCTTCTCCCATAGTTCCTTCCCTAGGTTTCGGAATGAGCCAAAAGGTG
GGCCATCTGGATTTCTTTCCAAATGGAGGAAAGGAAATGCCCGGATGTAAGAAAAATGTC
CTTTCAACCATTACTGATATTGATGGAATATGGGAAGGAATTGGTGGCTTTGTGTCTTGC
AATCACCTAAGAAGCTTCGAGTATTACTCAAGCAGCGTCCTCAACCCTGATGGCTTCCTG
GGCTATCCCTGTGCCTCCTACGATGAGTTTCAGGAGAGTAAGTGTTTCCCTTGTCCAGCT
GAAGGATGCCCCAAAATGGGGCACTATGCTGACCAATTTAAGGGGAAAACAAGTGCTGTG
GAACAAACCTTTTTCCTGAACACAGGAGAGAGTGGTAACTTTACTAGTTGGAGATATAAG
GTATCAGTCACACTTTCTGGAAAAGAGAAAGTGAATGGGTACATCAGGATTGCTTTGTAT
GGAAGTAATGAAAACTCGAAACAATATGAGATTTTCAAAGGATCCCTCAAACCAGATGCA
AGTCACACGTGTGCTATTGATGTGGATTTTAATGTTGGAAAAATACAGAAAGTTAAATTC
CTCTGGAACAAACGTGGGATAAATCTATCTGAGCCCAAACTGGGGGCTTCCCAAATCACA
GTGCAAAGTGGTGAAGATGGGACTGAGTATAATTTTTGTAGCAGCGACACTGTGGAAGAA
AACGTCTTGCAATCTCTTTACCCTTGTTAA
Enzyme 21 GenBank Gene ID M93284 Link Image
Enzyme 21 GeneCard ID PNLIPRP2 Link Image
Enzyme 21 GenAtlas ID PNLIPRP2 Link Image
Enzyme 21 HGNC ID HGNC:9157 Link Image
Enzyme 21 Chromosome Location 10
Enzyme 21 Locus 10q25.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5545
Enzyme 22 Name Lipoprotein lipase precursor
Enzyme 22 Synonyms
  1. LPL
Enzyme 22 Gene Name LPL
Enzyme 22 Protein Sequence >Lipoprotein lipase precursor
MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGV
AESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEH
YPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRIT
GLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQ
PGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKG
LCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQ
AFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDW
WSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG
Enzyme 22 Number of Residues 475
Enzyme 22 Molecular Weight 53163
Enzyme 22 Theoretical pI 8.26
Enzyme 22 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • lipoprotein lipase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). The enzyme functions in the presence of apolipoprotein C-2 on the luminal surface of vascular endothelium
Enzyme 22 Pathways
Enzyme 22 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • 1-27
Enzyme 22 Transmembrane Regions Not Available
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 307138 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P06858 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name LIPL_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1428 bp
ATGGAGAGCAAAGCCCTGCTCGTGCTGACTCTGGCCGTGTGGCTCCAGAGTCTGACCGCC
TCCCGCGGAGGGGTGGCCGCCGCCGACCAAAGAAGAGATTTTATCGACATCGAAAGTAAA
TTTGCCCTAAGGACCCCTGAAGACACAGCTGAGGACACTTGCCACCTCATTCCCGGAGTA
GCAGAGTCCGTGGCTACCTGTCATTTCAATCACAGCAGCAAAACCTTCATGGTGATCCAT
GGCTGGACGGTAACAGGAATGTATGAGAGTTGGGTGCCAAAACTTGTGGCCGCCCTGTAC
AAGAGAGAACCAGACTCCAATGTCATTGTGGTGGACTGGCTGTCACGGGCTCAGGAGCAT
TACCCAGTGTCCGCGGGCTACACCAAACTGGTGGGACAGGATGTGGCCCGGTTTATCAAC
TGGATGGAGGAGGAGTTTAACTACCCTCTGGACAATGTCCATCTCTTGGGATACAGCCTT
GGAGCCCATGCTGCTGGCATTGCAGGAAGTCTGACCAATAAGAAAGTCAACAGAATTACT
GGCCTCGATCCAGCTGGACCTAACTTTGAGTATGCAGAAGCCCCGAGTCGTCTTTCTCCT
GATGATGCAGATTTTGTAGACGTCTTACACACATTCACCAGAGGGTCCCCTGGTCGAAGC
ATTGGAATCCAGAAACCAGTTGGGCATGTTGACATTTACCCGAATGGAGGTACTTTTCAG
CCAGGATGTAACATTGGAGAAGCTATCCGCGTGATTGCAGAGAGAGGACTTGGAGATGTG
GACCAGCTAGTGAAGTGCTCCCACGAGCGCTCCATTCATCTCTTCATCGACTCTCTGTTG
AATGAAGAAAATCCAAGTAAGGCCTACAGGTGCAGTTCCAAGGAAGCCTTTGAGAAAGGG
CTCTGCTTGAGTTGTAGAAAGAACCGCTGCAACAATCTGGGCTATGAGATCAATAAAGTC
AGAGCCAAAAGAAGCAGCAAAATGTACCTGAAGACTCGTTCTCAGATGCCCTACAAAGTC
TTCCATTACCAAGTAAAGATTCATTTTTCTGGGACTGAGAGTGAAACCCATACCAATCAG
GCCTTTGAGATTTCTCTGTATGGCACCGTGGCCGAGAGTGAGAACATCCCATTCACTCTG
CCTGAAGTTTCCACAAATAAGACCTACTCCTTCCTAATTTACACAGAGGTAGATATTGGA
GAACTACTCATGTTGAAGCTCAAATGGAAGAGTGATTCATACTTTAGCTGGTCAGACTGG
TGGAGCAGTCCCGGCTTCGCCATTCAGAAGATCAGAGTAAAAGCAGGAGAGACTCAGAAA
AAGGTGATCTTCTGTTCTAGGGAGAAAGTGTCTCATTTGCAGAAAGGAAAGGCACCTGCG
GTATTTGTGAAATGCCATGACAAGTCTCTGAATAAGAAGTCAGGCTGA
Enzyme 22 GenBank Gene ID M15856 Link Image
Enzyme 22 GeneCard ID LPL Link Image
Enzyme 22 GenAtlas ID LPL Link Image
Enzyme 22 HGNC ID HGNC:6677 Link Image
Enzyme 22 Chromosome Location 8
Enzyme 22 Locus 8p22
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Wion KL, Kirchgessner TG, Lusis AJ, Schotz MC, Lawn RM: Human lipoprotein lipase complementary DNA sequence. Science. 1987 Mar 27;235(4796):1638-41. [PubMed Link Image]
  2. Gotoda T, Senda M, Gamou T, Furuichi Y, Oka K: Nucleotide sequence of human cDNA coding for a lipoprotein lipase (LPL) cloned from placental cDNA library. Nucleic Acids Res. 1989 Mar 25;17(6):2351. [PubMed Link Image]
  3. Takagi A, Ikeda Y, Yamamoto A: DNA sequence of lipoprotein lipase cDNA cloned from human monocytic leukemia THP-1 cells. Nucleic Acids Res. 1990 Nov 11;18(21):6436. [PubMed Link Image]
  4. Chuat JC, Raisonnier A, Etienne J, Galibert F: The lipoprotein lipase-encoding human gene: sequence from intron-6 to intron-9 and presence in intron-7 of a 40-million-year-old Alu sequence. Gene. 1992 Jan 15;110(2):257-61. [PubMed Link Image]
  5. Enerback S, Ohlsson BG, Samuelsson L, Bjursell G: Characterization of the human lipoprotein lipase (LPL) promoter: evidence of two cis-regulatory regions, LP-alpha and LP-beta, of importance for the differentiation-linked induction of the LPL gene during adipogenesis. Mol Cell Biol. 1992 Oct;12(10):4622-33. [PubMed Link Image]
  6. Zechner R: Rapid and simple isolation procedure for lipoprotein lipase from human milk. Biochim Biophys Acta. 1990 May 1;1044(1):20-5. [PubMed Link Image]
  7. Emmerich J, Beg OU, Peterson J, Previato L, Brunzell JD, Brewer HB Jr, Santamarina-Fojo S: Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241. J Biol Chem. 1992 Feb 25;267(6):4161-5. [PubMed Link Image]
  8. van Tilbeurgh H, Roussel A, Lalouel JM, Cambillau C: Lipoprotein lipase. Molecular model based on the pancreatic lipase x-ray structure: consequences for heparin binding and catalysis. J Biol Chem. 1994 Feb 11;269(6):4626-33. [PubMed Link Image]
  9. Wilson DE, Hata A, Kwong LK, Lingam A, Shuhua J, Ridinger DN, Yeager C, Kaltenborn KC, Iverius PH, Lalouel JM: Mutations in exon 3 of the lipoprotein lipase gene segregating in a family with hypertriglyceridemia, pancreatitis, and non-insulin-dependent diabetes. J Clin Invest. 1993 Jul;92(1):203-11. [PubMed Link Image]
  10. Ishimura-Oka K, Faustinella F, Kihara S, Smith LC, Oka K, Chan L: A missense mutation (Trp86----Arg) in exon 3 of the lipoprotein lipase gene: a cause of familial chylomicronemia. Am J Hum Genet. 1992 Jun;50(6):1275-80. [PubMed Link Image]
  11. Reina M, Brunzell JD, Deeb SS: Molecular basis of familial chylomicronemia: mutations in the lipoprotein lipase and apolipoprotein C-II genes. J Lipid Res. 1992 Dec;33(12):1823-32. [PubMed Link Image]
  12. Ameis D, Kobayashi J, Davis RC, Ben-Zeev O, Malloy MJ, Kane JP, Lee G, Wong H, Havel RJ, Schotz MC: Familial chylomicronemia (type I hyperlipoproteinemia) due to a single missense mutation in the lipoprotein lipase gene. J Clin Invest. 1991 Apr;87(4):1165-70. [PubMed Link Image]
  13. Bruin T, Tuzgol S, van Diermen DE, Hoogerbrugge-van der Linden N, Brunzell JD, Hayden MR, Kastelein JJ: Recurrent pancreatitis and chylomicronemia in an extended Dutch kindred is caused by a Gly154-->Ser substitution in lipoprotein lipase. J Lipid Res. 1993 Dec;34(12):2109-19. [PubMed Link Image]
  14. Ma YH, Bruin T, Tuzgol S, Wilson BI, Roederer G, Liu MS, Davignon J, Kastelein JJ, Brunzell JD, Hayden MR: Two naturally occurring mutations at the first and second bases of codon aspartic acid 156 in the proposed catalytic triad of human lipoprotein lipase. In vivo evidence that aspartic acid 156 is essential for catalysis. J Biol Chem. 1992 Jan 25;267(3):1918-23. [PubMed Link Image]
  15. Faustinella F, Chang A, Van Biervliet JP, Rosseneu M, Vinaimont N, Smith LC, Chen SH, Chan L: Catalytic triad residue mutation (Asp156----Gly) causing familial lipoprotein lipase deficiency. Co-inheritance with a nonsense mutation (Ser447----Ter) in a Turkish family. J Biol Chem. 1991 Aug 5;266(22):14418-24. [PubMed Link Image]
  16. Bruin T, Kastelein JJ, Van Diermen DE, Ma Y, Henderson HE, Stuyt PM, Stalenhoef AF, Sturk A, Brunzell JD, Hayden MR: A missense mutation Pro157 Arg in lipoprotein lipase (LPLNijmegen) resulting in loss of catalytic activity. Eur J Biochem. 1992 Sep 1;208(2):267-72. [PubMed Link Image]
  17. Ma Y, Liu MS, Ginzinger D, Frohlich J, Brunzell JD, Hayden MR: Gene-environment interaction in the conversion of a mild-to-severe phenotype in a patient homozygous for a Ser172-->Cys mutation in the lipoprotein lipase gene. J Clin Invest. 1993 May;91(5):1953-8. [PubMed Link Image]
  18. Beg OU, Meng MS, Skarlatos SI, Previato L, Brunzell JD, Brewer HB Jr, Fojo SS: Lipoprotein lipaseBethesda: a single amino acid substitution (Ala-176----Thr) leads to abnormal heparin binding and loss of enzymic activity. Proc Natl Acad Sci U S A. 1990 May;87(9):3474-8. [PubMed Link Image]
  19. Haubenwallner S, Horl G, Shachter NS, Presta E, Fried SK, Hofler G, Kostner GM, Breslow JL, Zechner R: A novel missense mutation in the gene for lipoprotein lipase resulting in a highly conservative amino acid substitution (Asp180-->Glu) causes familial chylomicronemia (type I hyperlipoproteinemia). Genomics. 1993 Nov;18(2):392-6. [PubMed Link Image]
  20. Emi M, Wilson DE, Iverius PH, Wu L, Hata A, Hegele R, Williams RR, Lalouel JM: Missense mutation (Gly----Glu188) of human lipoprotein lipase imparting functional deficiency. J Biol Chem. 1990 Apr 5;265(10):5910-6. [PubMed Link Image]
  21. Monsalve MV, Henderson H, Roederer G, Julien P, Deeb S, Kastelein JJ, Peritz L, Devlin R, Bruin T, Murthy MR, et al.: A missense mutation at codon 188 of the human lipoprotein lipase gene is a frequent cause of lipoprotein lipase deficiency in persons of different ancestries. J Clin Invest. 1990 Sep;86(3):728-34. [PubMed Link Image]
  22. Ishimura-Oka K, Semenkovich CF, Faustinella F, Goldberg IJ, Shachter N, Smith LC, Coleman T, Hide WA, Brown WV, Oka K, et al.: A missense (Asp250----Asn) mutation in the lipoprotein lipase gene in two unrelated families with familial lipoprotein lipase deficiency. J Lipid Res. 1992 May;33(5):745-54. [PubMed Link Image]
  23. Henderson HE, Ma Y, Hassan MF, Monsalve MV, Marais AD, Winkler F, Gubernator K, Peterson J, Brunzell JD, Hayden MR: Amino acid substitution (Ile194----Thr) in exon 5 of the lipoprotein lipase gene causes lipoprotein lipase deficiency in three unrelated probands. Support for a multicentric origin. J Clin Invest. 1991 Jun;87(6):2005-11. [PubMed Link Image]
  24. Dichek HL, Fojo SS, Beg OU, Skarlatos SI, Brunzell JD, Cutler GB Jr, Brewer HB Jr: Identification of two separate allelic mutations in the lipoprotein lipase gene of a patient with the familial hyperchylomicronemia syndrome. J Biol Chem. 1991 Jan 5;266(1):473-7. [PubMed Link Image]
  25. Hata A, Ridinger DN, Sutherland SD, Emi M, Kwong LK, Shuhua J, Lubbers A, Guy-Grand B, Basdevant A, Iverius PH, et al.: Missense mutations in exon 5 of the human lipoprotein lipase gene. Inactivation correlates with loss of dimerization. J Biol Chem. 1992 Oct 5;267(28):20132-9. [PubMed Link Image]
  26. Gotoda T, Yamada N, Kawamura M, Kozaki K, Mori N, Ishibashi S, Shimano H, Takaku F, Yazaki Y, Furuichi Y, et al.: Heterogeneous mutations in the human lipoprotein lipase gene in patients with familial lipoprotein lipase deficiency. J Clin Invest. 1991 Dec;88(6):1856-64. [PubMed Link Image]
  27. Ma Y, Henderson HE, Murthy V, Roederer G, Monsalve MV, Clarke LA, Normand T, Julien P, Gagne C, Lambert M, et al.: A mutation in the human lipoprotein lipase gene as the most common cause of familial chylomicronemia in French Canadians. N Engl J Med. 1991 Jun 20;324(25):1761-6. [PubMed Link Image]
  28. Hata A, Emi M, Luc G, Basdevant A, Gambert P, Iverius PH, Lalouel JM: Compound heterozygote for lipoprotein lipase deficiency: Ser----Thr244 and transition in 3' splice site of intron 2 (AG----AA) in the lipoprotein lipase gene. Am J Hum Genet. 1990 Oct;47(4):721-6. [PubMed Link Image]
  29. Ma Y, Wilson BI, Bijvoet S, Henderson HE, Cramb E, Roederer G, Ven Murthy MR, Julien P, Bakker HD, Kastelein JJ, et al.: A missense mutation (Asp250----Asn) in exon 6 of the human lipoprotein lipase gene causes chylomicronemia in patients of different ancestries. Genomics. 1992 Jul;13(3):649-53. [PubMed Link Image]
  30. Reymer PW, Gagne E, Groenemeyer BE, Zhang H, Forsyth I, Jansen H, Seidell JC, Kromhout D, Lie KE, Kastelein J, et al.: A lipoprotein lipase mutation (Asn291Ser) is associated with reduced HDL cholesterol levels in premature atherosclerosis. Nat Genet. 1995 May;10(1):28-34. [PubMed Link Image]
  31. Kobayashi J, Sasaki N, Tashiro J, Inadera H, Saito Y, Yoshida S: A missense mutation (Ala334-->Thr) in exon 7 of the lipoprotein lipase gene in a case with type I hyperlipidemia. Biochem Biophys Res Commun. 1993 Mar 31;191(3):1046-54. [PubMed Link Image]
  32. Pepe G, Chimienti G, Resta F, Di Perna V, Tarricone C, Lovecchio M, Colacicco AM, Capurso A: A new Italian case of lipoprotein lipase deficiency: a Leu365- > Val change resulting in loss of enzyme activity. Biochem Biophys Res Commun. 1994 Mar 15;199(2):570-6. [PubMed Link Image]
  33. Previato L, Guardamagna O, Dugi KA, Ronan R, Talley GD, Santamarina-Fojo S, Brewer HB Jr: A novel missense mutation in the C-terminal domain of lipoprotein lipase (Glu410-->Val) leads to enzyme inactivation and familial chylomicronemia. J Lipid Res. 1994 Sep;35(9):1552-60. [PubMed Link Image]
  34. Wiebusch H, Funke H, Bruin T, Bucher H, von Eckardstein A, Kastelein JJ, Assmann G: Compound heterozygosity for a known (D250N) and a novel (E410K) missense mutation in the C-terminal domain of lipoprotein lipase causes familial chylomicronemia. Hum Mutat. 1996;8(4):381-3. [PubMed Link Image]
  35. Foubert L, Bruin T, De Gennes JL, Ehrenborg E, Furioli J, Kastelein J, Benlian P, Hayden M: A single Ser259Arg mutation in the gene for lipoprotein lipase causes chylomicronemia in Moroccans of Berber ancestry. Hum Mutat. 1997;10(3):179-85. [PubMed Link Image]
  36. Mailly F, Palmen J, Muller DP, Gibbs T, Lloyd J, Brunzell J, Durrington P, Mitropoulos K, Betteridge J, Watts G, Lithell H, Angelico F, Humphries SE, Talmud PJ: Familial lipoprotein lipase (LPL) deficiency: a catalogue of LPL gene mutations identified in 20 patients from the UK, Sweden, and Italy. Hum Mutat. 1997;10(6):465-73. [PubMed Link Image]
  37. Zhang Q, Liu Y, Liu BW, Fan P, Cavanna J, Galton DJ: Common genetic variants of lipoprotein lipase and apolipoproteins AI-CIII that relate to coronary artery disease: a study in Chinese and European subjects. Mol Genet Metab. 1998 Jul;64(3):177-83. [PubMed Link Image]
  38. Nickerson DA, Taylor SL, Weiss KM, Clark AG, Hutchinson RG, Stengard J, Salomaa V, Vartiainen E, Boerwinkle E, Sing CF: DNA sequence diversity in a 9.7-kb region of the human lipoprotein lipase gene. Nat Genet. 1998 Jul;19(3):233-40. [PubMed Link Image]
  39. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  40. Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5744
Enzyme 23 Name Liver carboxylesterase 1 precursor
Enzyme 23 Synonyms
  1. Acyl coenzyme A:cholesterol acyltransferase
  2. ACAT
  3. Monocyte/macrophage serine esterase
  4. HMSE
  5. Serine esterase 1
  6. Brain carboxylesterase hBr1
  7. Triacylglycerol hydrolase
  8. TGH
  9. Egasyn
Enzyme 23 Gene Name CES1
Enzyme 23 Protein Sequence >Liver carboxylesterase 1 precursor
MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPL
GPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLN
IYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST
GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLF
HRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLK
MKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIP
MQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDL
IADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPF
LKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLK
DKEVAFWTNLFAKKAVEKPPQTEHIEL
Enzyme 23 Number of Residues 567
Enzyme 23 Molecular Weight 62522
Enzyme 23 Theoretical pI 6.58
Enzyme 23 GO Classification Not Available
Enzyme 23 General Function Lipid transport and metabolism
Enzyme 23 Specific Function Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl CoA ester
Enzyme 23 Pathways
Enzyme 23 Reactions
  • A carboxylic ester + H2O = an alcohol + a carboxylate
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-18
Enzyme 23 Transmembrane Regions Not Available
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 179928 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID P23141 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name EST1_HUMAN Link Image
Enzyme 23 PDB ID 1MX1 Link Image
Enzyme 23 PDB File Show
Enzyme 23 3D Structure
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1704 bp
ATGTGGCTCCGTGCCTTTATCCTGGCCACTCTCTCTGCTTCCGCGGCTTGGGGGCATCCG
TCCTCGCCACCTGTGGTGGACACCGTGCATGGCAAAGTGCTGGGGAAGTTCGTCAGCTTA
GAAGGATTTGCACAGCCTGTGGCCATTTTCCTGGGAATCCCTTTTGCCAAGCCGCCTCTT
GGACCCCTGAGGTTTACTCCACCGCAGCCTGCAGAACCATGGAGCTTTGTGAAGAATGCC
ACCTCGTACCCTCCTATGTGCACCCAAGATCCCAAGGCGGGGCAGTTACTCTCAGAGCTA
TTTACAAACCGAAAGGAGAACATTCCTCTCAAGCTTTCTGAAGACTGTCTTTACCTCAAT
ATTTACACTCCTGCTGACTTGACCAAGAAAAACAGGCTGCCGGTGATGGTGTGGATCCAC
GGAGGGGGGCTGATGGTGGGTGCGGCATCAACCTATGATGGGCTGGCCCTTGCTGCCCAT
GAAAACGTGGTGGTGGTGACCATTCAATATCGCCTGGGCATCTGGGGATTCTTCAGCACA
GGGGATGAACACAGCCGGGGGAACTGGGGTCACCTGGACCAGGTGGCTGCCCTGCGCTGG
GTCCAGGACAACATTGCCAGCTTTGGAGGGAACCCAGGCTCTGTGACCATCTTTGGAGAG
TCAGCGGGAGGAGAAAGTGTCTCTGTTCTTGTTTTGTCTCCATTGGCCAAGAACCTCTTC
CACCGGGCCATTTCTGAGAGTGGCGTGGCCCTCACTTCTGTTCTGGTGAAGAAAGGTGAT
GTCAAGCCCTTGGCTGAGCAAATTGCTATCACTGCTGGGTGCAAAACCACCACCTCTGCT
GTCATGGTTCACTGCCTGCGACAGAAGACGGAAGAGGAGCTCTTGGAGACGACATTGAAA
ATGAAATTCTTATCTCTGGACTTACAGGGAGACCCCAGAGAGAGTCAACCCCTTCTGGGC
ACTGTGATTGATGGGATGCTGCTGCTGAAAACACCTGAAGAGCTTCAAGCTGAAAGGAAT
TTCCACACTGTCCCCTACATGGTCGGAATTAACAAGCAGGAGTTTGGCTGGTTGATTCCA
ATGCAGTTGATGAGCTATCCACTCTCCGAAGGGCAACTGGACCAGAAGACAGCCATGTCA
CTCCTGTGGAAGTCCTATCCCCTTGTTTGCATTGCTAAGGAACTGATTCCAGAAGCCACT
GAGAAATACTTAGGAGGAACAGACGACACTGTCAAAAAGAAAGACCTGTTCCTGGACTTG
ATAGCAGATGTGATGTTTGGTGTCCCATCTGTGATTGTGGCCCGGAACCACAGAGATGCT
GGAGCACCCACCTACATGTATGAGTTTCAGTACCGTCCAAGCTTCTCATCAGACATGAAA
CCCAAGACGGTGATAGGAGACCACGGGGATGAGCTCTTCTCCGTCTTTGGGGCCCCATTT
TTAAAAGAGGGTGCCTCAGAAGAGGAGATCAGACTTAGCAAGATGGTGATGAAATTCTGG
GCCAACTTTGCTCGCAATGGAAACCCCAATGGGGAAGGGCTGCCCCACTGGCCAGAGTAC
AACCAGAAGGAAGGGTATCTGCAGATTGGTGCCAACACCCAGGCGGCCCAGAAGCTGAAG
GACAAAGAAGTAGCTTTCTGGACCAACCTCTTTGCCAAGAAGGCAGTGGAGAAGCCACCC
CAGACAGAACACATAGAGCTGTGA
Enzyme 23 GenBank Gene ID M73499 Link Image
Enzyme 23 GeneCard ID CES1 Link Image
Enzyme 23 GenAtlas ID CES1 Link Image
Enzyme 23 HGNC ID HGNC:1863 Link Image
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Munger JS, Shi GP, Mark EA, Chin DT, Gerard C, Chapman HA: A serine esterase released by human alveolar macrophages is closely related to liver microsomal carboxylesterases. J Biol Chem. 1991 Oct 5;266(28):18832-8. [PubMed Link Image]
  2. Kroetz DL, McBride OW, Gonzalez FJ: Glycosylation-dependent activity of baculovirus-expressed human liver carboxylesterases: cDNA cloning and characterization of two highly similar enzyme forms. Biochemistry. 1993 Nov 2;32(43):11606-17. [PubMed Link Image]
  3. Shibata F, Takagi Y, Kitajima M, Kuroda T, Omura T: Molecular cloning and characterization of a human carboxylesterase gene. Genomics. 1993 Jul;17(1):76-82. [PubMed Link Image]
  4. Becker A, Bottcher A, Lackner KJ, Fehringer P, Notka F, Aslanidis C, Schmitz G: Purification, cloning, and expression of a human enzyme with acyl coenzyme A: cholesterol acyltransferase activity, which is identical to liver carboxylesterase. Arterioscler Thromb. 1994 Aug;14(8):1346-55. [PubMed Link Image]
  5. Ghosh S: Cholesteryl ester hydrolase in human monocyte/macrophage: cloning, sequencing, and expression of full-length cDNA. Physiol Genomics. 2000 Jan 24;2(1):1-8. [PubMed Link Image]
  6. Mori M, Hosokawa M, Ogasawara Y, Tsukada E, Chiba K: cDNA cloning, characterization and stable expression of novel human brain carboxylesterase. FEBS Lett. 1999 Sep 10;458(1):17-22. [PubMed Link Image]
  7. Long RM, Calabrese MR, Martin BM, Pohl LR: Cloning and sequencing of a human liver carboxylesterase isoenzyme. Life Sci. 1991;48(11):PL43-9. [PubMed Link Image]
  8. Zschunke F, Salmassi A, Kreipe H, Buck F, Parwaresch MR, Radzun HJ: cDNA cloning and characterization of human monocyte/macrophage serine esterase-1. Blood. 1991 Jul 15;78(2):506-12. [PubMed Link Image]
  9. Riddles PW, Richards LJ, Bowles MR, Pond SM: Cloning and analysis of a cDNA encoding a human liver carboxylesterase. Gene. 1991 Dec 15;108(2):289-92. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5745
Enzyme 24 Name Carboxylesterase 2 precursor
Enzyme 24 Synonyms
  1. CE-2
  2. hCE-2
Enzyme 24 Gene Name CES2
Enzyme 24 Protein Sequence >Carboxylesterase 2 precursor
MRLHRLRARLSAVACGLLLLLVRGQGQDSASPIRTTHTGQVLGSLVHVKGANAGVQTFLG
IPFAKPPLGPLRFAPPEPPESWSGVRDGTTHPAMCLQDLTAVESEFLSQFNMTFPSDSMS
EDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDGSMLAALENVVVVIIQYRLG
VLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVS
PISQGLFHGAIMESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEI
LAINKPFKMIPGVVDGVFLPRHPQELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQ
KEMDREASQAALQKMLTLLMLPPTFGDLLREEYIGDNGDPQTLQAQFQEMMADSMFVIPA
LQVAHFQCSRAPVYFYEFQHQPSWLKNIRPPHMKADHGDELPFVFRSFFGGNYIKFTEEE
EQLSRKMMKYWANFARNGNPNGEGLPHWPLFDQEEQYLQLNLQPAVGRALKAHRLQFWKK
ALPQKIQELEEPEERHTEL
Enzyme 24 Number of Residues 559
Enzyme 24 Molecular Weight 61808
Enzyme 24 Theoretical pI 6.03
Enzyme 24 GO Classification Not Available
Enzyme 24 General Function Lipid transport and metabolism
Enzyme 24 Specific Function Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows high catalytic efficiency for hydrolysis of 4-methyumbelliferyl acetate, heroin and 6-monoacetylmorphine
Enzyme 24 Pathways
Enzyme 24 Reactions
  • A carboxylic ester + H2O = an alcohol + a carboxylate
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • 1-26
Enzyme 24 Transmembrane Regions Not Available
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 2058318 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID O00748 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name EST2_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1680 bp
ATGCGGCTGCACAGACTTCGTGCGCGGCTGAGCGCGGTGGCCTGTGGGCTTCTGCTGCTT
CTTGTCCGGGGCCAGGGCCAGGACTCAGCCAGTCCCATCCGGACCACACACACGGGGCAG
GTGCTGGGGAGTCTTGTCCATGTGAAGGGCGCCAATGCCGGGGTCCAAACCTTCCTGGGA
ATTCCATTTGCCAAGCCACCTCTAGGTCCGCTGCGATTTGCACCCCCTGAGCCCCCTGAA
TCTTGGAGTGGTGTGAGGGATGGAACCACCCATCCGGCCATGTGTCTACAGGACCTCACC
GCAGTGGAGTCAGAGTTTCTTAGCCAGTTCAACATGACCTTCCCTTCCGACTCCATGTCT
GAGGACTGCCTGTACCTCAGCATCTACACGCCGGCCCATAGCCATGAAGGCTCTAACCTG
CCGGTGATGGTGTGGATCCACGGTGGTGCGCTTGTTTTTGGCATGGCTTCCTTGTATGAT
GGTTCCATGCTGGCTGCCTTGGAGAACGTGGTGGTGGTCATCATCCAGTACCGCCTGGGT
GTCCTGGGCTTCTTCAGCACTGGAGACAAGCACGCAACCGGCAACTGGGGCTACCTGGAC
CAAGTGGCTGCACTACGCTGGGTCCAGCAGAATATCGCCCACTTTGGAGGCAACCCTGAC
CGTGTCACCATTTTTGGCGAGTCTGCGGGTGGCACGAGTGTGTCTTCGCTTGTTGTGTCC
CCCATATCCCAAGGACTCTTCCACGGAGCCATCATGGAGAGTGGCGTGGCCCTCCTGCCC
GGCCTCATTGCCAGCTCAGCTGATGTCATCTCCACGGTGGTGGCCAACCTGTCTGCCTGT
GACCAAGTTGACTCTGAGGCCCTGGTGGGCTGCCTGCGGGGCAAGAGTAAAGAGGAGATT
CTTGCAATTAACAAGCCTTTCAAGATGATCCCCGGAGTGGTGGATGGGGTCTTCCTGCCC
AGGCACCCCCAGGAGCTGCTGGCCTCTGCCGACTTTCAGCCTGTCCCTAGCATTGTTGGT
GTCAACAACAATGAATTCGGCTGGCTCATCCCCAAGGTCATGAGGATCTATGATACCCAG
AAGGAAATGGACAGAGAGGCCTCCCAGGCTGCTCTGCAGAAAATGTTAACGCTGCTGATG
TTGCCTCCTACATTTGGTGACCTGCTGAGGGAGGAGTACATTGGGGACAATGGGGATCCC
CAGACCCTCCAAGCGCAGTTCCAGGAGATGATGGCGGACTCCATGTTTGTGATCCCTGCA
CTCCAAGTAGCACATTTTCAGTGTTCCCGGGCCCCTGTGTACTTCTACGAGTTCCAGCAT
CAGCCCAGCTGGCTCAAGAACATCAGGCCACCGCACATGAAGGCAGACCATGGTGATGAG
CTTCCTTTTGTTTTCAGAAGTTTCTTTGGGGGCAACTACATTAAATTCACTGAGGAAGAG
GAGCAGCTAAGCAGGAAGATGATGAAGTACTGGGCCAACTTTGCGAGAAATGGGAACCCC
AATGGCGAGGGTCTGCCACACTGGCCGCTGTTCGACCAGGAGGAGCAATACCTGCAGCTG
AACCTACAGCCTGCGGTGGGCCGGGCTCTGAAGGCCCACAGGCTCCAGTTCTGGAAGAAG
GCGCTGCCCCAAAAGATCCAGGAGCTCGAGGAGCCTGAAGAGAGACACACAGAGCTGTAG
Enzyme 24 GenBank Gene ID Y09616 Link Image
Enzyme 24 GeneCard ID CES2 Link Image
Enzyme 24 GenAtlas ID CES2 Link Image
Enzyme 24 HGNC ID HGNC:1864 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Schwer H, Langmann T, Daig R, Becker A, Aslanidis C, Schmitz G: Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver. Biochem Biophys Res Commun. 1997 Apr 7;233(1):117-20. [PubMed Link Image]
  2. Pindel EV, Kedishvili NY, Abraham TL, Brzezinski MR, Zhang J, Dean RA, Bosron WF: Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin. J Biol Chem. 1997 Jun 6;272(23):14769-75. [PubMed Link Image]
  3. Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5774
Enzyme 25 Name Cholinesterase precursor
Enzyme 25 Synonyms
  1. Acylcholine acylhydrolase
  2. Choline esterase II
  3. Butyrylcholine esterase
  4. Pseudocholinesterase
Enzyme 25 Gene Name BCHE
Enzyme 25 Protein Sequence >Cholinesterase precursor
MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP
YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC
LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG
FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG
SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI
LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY
GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV
VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER
RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT
KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV
GL
Enzyme 25 Number of Residues 602
Enzyme 25 Molecular Weight 68419
Enzyme 25 Theoretical pI 7.47
Enzyme 25 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cholinesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
Component
Enzyme 25 General Function Lipid transport and metabolism
Enzyme 25 Specific Function An acylcholine + H(2)O = choline + a carboxylate
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions
  • An acylcholine + H2O = choline + a carboxylate
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • 1-28
Enzyme 25 Transmembrane Regions
  • 45-67
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 1311630 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P06276 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name CHLE_HUMAN Link Image
Enzyme 25 PDB ID 1P0Q Link Image
Enzyme 25 PDB File Show
Enzyme 25 3D Structure
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1809 bp
ATGCATAGCAAAGTCACAATCATATGCATCAGATTTCTCTTTTGGTTTCTTTTGCTCTGC
ATGCTTATTGGGAAGTCACATACTGAAGATGACATCATAATTGCAACAAAGAATGGAAAA
GTCAGAGGGATGAACTTGACAGTTTTTGGTGGCACGGTAACAGCCTTTCTTGGAATTCCC
TATGCACAGCCACCTCTTGGTAGACTTCGATTCAAAAAGCCACAGTCTCTGACCAAGTGG
TCTGATATTTGGAATGCCACAAAATATGCAAATTCTTGCTGTCAGAACATAGATCAAAGT
TTTCCAGGCTTCCATGGATCAGAGATGTGGAACCCAAACACTGACCTCAGTGAAGACTGT
TTATATCTAAATGTATGGATTCCAGCACCTAAACCAAAAAATGCCACTGTATTGATATGG
ATTTATGGTGGTGGTTTTCAAACTGGAACATCATCTTTACATGTTTATGATGGCAAGTTT
CTGGCTCGGGTTGAAAGAGTTATTGTAGTGTCAATGAACTATAGGGTGGGTGCCCTAGGA
TTCTTAGCTTTGCCAGGAAATCCTGAGGCTCCAGGGAACATGGGTTTATTTGATCAACAG
TTGGCTCTTCAGTGGGTTCAAAAAAATATAGCAGCCTTTGGTGGAAATCCTAAAAGTGTA
ACTCTCTTTGGAGAAAGTGCAGGAGCAGCTTCAGTTAGCCTGCATTTGCTTTCTCCTGGA
AGCCATTCATTGTTCACCAGAGCCATTCTGCAAAGTGGATCCTTTAATGCTCCTTGGGCG
GTAACATCTCTTTATGAAGCTAGGAACAGAACGTTGAACTTAGCTAAATTGACTGGTTGC
TCTAGAGAGAATGAGACTGAAATAATCAAGTGTCTTAGAAATAAAGATCCCCAAGAAATT
CTTCTGAATGAAGCATTTGTTGTCCCCTATGGGACTCCTTTGTCAGTAAACTTTGGTCCG
ACCGTGGATGGTGATTTTCTCACTGACATGCCAGACATATTACTTGAACTTGGACAATTT
AAAAAAACCCAGATTTTGGTGGGTGTTAATAAAGATGAAGGGACAGCTTTTTTAGTCTAT
GGTGCTCCTGGCTTCAGCAAAGATAACAATAGTATCATAACTAGAAAAGAATTTCAGGAA
GGTTTAAAAATATTTTTTCCAGGAGTGAGTGAGTTTGGAAAGGAATCCATCCTTTTTCAT
TACACAGACTGGGTAGATGATCAGAGACCTGAAAACTACCGTGAGGCCTTGGGTGATGTT
GTTGGGGATTATAATTTCATATGCCCTGCCTTGGAGTTCACCAAGAAGTTCTCAGAATGG
GGAAATAATGCCTTTTTCTACTATTTTGAACACCGATCCTCCAAACTTCCGTGGCCAGAA
TGGATGGGAGTGATGCATGGCTATGAAATTGAATTTGTCTTTGGTTTACCTCTGGAAAGA
AGAGATAATTACACAAAAGCCGAGGAAATTTTGAGTAGATCCATAGTGAAACGTTGGGCA
AATTTTGCAAAATATGGGAATCCAAATGAGACTCAGAACAATAGCACAAGCTGGCCTGTC
TTCAAAAGCACTGAACAAAAATATCTAACCTTGAATACAGAGTCAACAAGAATAATGACG
AAACTACGTGCTCAACAATGTCGATTCTGGACATCATTTTTTCCAAAAGTCTTGGAAATG
ACAGGAAATATTGATGAAGCAGAATGGGAGTGGAAAGCAGGATTCCATCGCTGGAACAAT
TACATGATGGACTGGAAAAATCAATTTAACGATTACACTAGCAAGAAAGAAAGTTGTGTG
GGTCTCTAA
Enzyme 25 GenBank Gene ID M32391 Link Image
Enzyme 25 GeneCard ID BCHE Link Image
Enzyme 25 GenAtlas ID BCHE Link Image
Enzyme 25 HGNC ID HGNC:983 Link Image
Enzyme 25 Chromosome Location 3
Enzyme 25 Locus 3q26.1-q26.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Arpagaus M, Kott M, Vatsis KP, Bartels CF, La Du BN, Lockridge O: Structure of the gene for human butyrylcholinesterase. Evidence for a single copy. Biochemistry. 1990 Jan 9;29(1):124-31. [PubMed Link Image]
  2. Prody CA, Zevin-Sonkin D, Gnatt A, Goldberg O, Soreq H: Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3555-9. [PubMed Link Image]
  3. McTiernan C, Adkins S, Chatonnet A, Vaughan TA, Bartels CF, Kott M, Rosenberry TL, La Du BN, Lockridge O: Brain cDNA clone for human cholinesterase. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6682-6. [PubMed Link Image]
  4. Lockridge O, Bartels CF, Vaughan TA, Wong CK, Norton SE, Johnson LL: Complete amino acid sequence of human serum cholinesterase. J Biol Chem. 1987 Jan 15;262(2):549-57. [PubMed Link Image]
  5. Lockridge O, Adkins S, La Du BN: Location of disulfide bonds within the sequence of human serum cholinesterase. J Biol Chem. 1987 Sep 25;262(27):12945-52. [PubMed Link Image]
  6. Lockridge O: Structure of human serum cholinesterase. Bioessays. 1988 Oct;9(4):125-8. [PubMed Link Image]
  7. McGuire MC, Nogueira CP, Bartels CF, Lightstone H, Hajra A, Van der Spek AF, Lockridge O, La Du BN: Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase. Proc Natl Acad Sci U S A. 1989 Feb;86(3):953-7. [PubMed Link Image]
  8. Iida S, Kinoshita M, Fujii H, Moriyama Y, Nakamura Y, Yura N, Moriwaki K: Mutations of human butyrylcholinesterase gene in a family with hypocholinesterasemia. Hum Mutat. 1995;6(4):349-51. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5778
Enzyme 26 Name Cytosolic phospholipase A2 gamma precursor
Enzyme 26 Synonyms
  1. cPLA2-gamma
  2. Phospholipase A2 group IVC
Enzyme 26 Gene Name PLA2G4C
Enzyme 26 Protein Sequence >Cytosolic phospholipase A2 gamma precursor
MGSSEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACL
GVLSEMKEQGLLDAVTYLAGVSGSTWAISSLYTNDGDMEALEADLKHRFTRQEWDLAKSL
QKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKKPVEEGTLPYPIFAAIDNDLQ
PSWQEARAPETWFEFTPHHAGFPALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWG
SALGNTEVIREYIFDQLRNLTLKGLWRRAVANAKSIGHLIFARLLRLQESSQGEHPPPED
EGGEPEHTWLTEMLENWTRTSLEKQEQPHEDPERKGSLSNLMDFVKKTGICASKWEWGTT
HNFLYKHGGIRDKIMSSRKHLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGDPFET
IRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDIE
AWSDTYDTFKLADTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLYYPKDSARSCCL
A
Enzyme 26 Number of Residues 541
Enzyme 26 Molecular Weight 60949
Enzyme 26 Theoretical pI 6.93
Enzyme 26 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase activity
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid catabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 26 General Function Not Available
Enzyme 26 Specific Function Has a preference for arachidonic acid at the sn-2 position of phosphatidylcholine as compared with palmitic acid
Enzyme 26 Pathways
Enzyme 26 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 3452315 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q9UP65 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name PA24C_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1626 bp
ATGGGAAGCTCTGAAGTTTCCATAATTCCTGGGCTCCAGAAAGAAGAAAAGGCGGCCGTG
GAGAGACGAAGACTTCATGTGCTGAAAGCTCTGAAGAAGCTAAGGATTGAGGCTGATGAG
GCCCCAGTTGTTGCTGTGCTGGGCTCAGGCGGAGGACTGCGGGCTCACATTGCCTGCCTT
GGGGTCCTGAGTGAGATGAAAGAACAGGGCCTGTTGGATGCCGTCACGTACCTCGCAGGG
GTCTCTGGATCCACTTGGGCAATATCTTCTCTCTACACCAATGATGGTGACATGGAAGCT
CTCGAGGCTGACCTGAAACATCGATTTACCCGACAGGAGTGGGACTTGGCTAAGAGCCTA
CAGAAAACCATCCAAGCAGCGAGGTCTGAGAATTACTCTCTGACCGACTTCTGGGCCTAC
ATGGTTATCTCTAAGCAAACCAGAGAACTGCCGGAGTCTCATTTGTCCAATATGAAGAAG
CCCGTGGAAGAAGGGACACTACCCTACCCAATATTTGCAGCCATTGACAATGACCTGCAA
CCTTCCTGGCAGGAGGCAAGAGCACCAGAGACCTGGTTCGAGTTCACCCCTCACCACGCT
GGCTTCTCTGCACTGGGGGCCTTTGTTTCCATAACCCACTTCGGAAGCAAATTCAAGAAG
GGAAGACTGGTCAGAACTCACCCTGAGAGAGACCTGACTTTCCTGAGAGGTTTATGGGGA
AGTGCTCTTGGTAACACTGAAGTCATTAGGGAATACATTTTTGACCAGTTAAGGAATCTG
ACCCTGAAAGGTTTATGGAGAAGGGCTGTTGCTAATGCTAAAAGCATTGGACACCTTATT
TTTGCCCGATTACTGAGGCTGCAAGAAAGTTCACAAGGGGAACATCCTCCCCCAGAAGAT
GAAGGCGGTGAGCCTGAACACACCTGGCTGACTGAGATGCTCGAGAATTGGACCAGGACC
TCCCTGGAAAAGCAGGAGCAGCCCCATGAGGACCCCGAAAGGAAAGGCTCACTCAGTAAC
TTGATGGATTTTGTGAAGAAAACAGGCATTTGCGCTTCAAAGTGGGAATGGGGGACCACT
CACAACTTCCTGTACAAACACGGTGGCATCCGGGACAAGATAATGAGCAGCCGGAAGCAC
CTCCACCTGGTGGATGCTGGTTTAGCCATCAACACTCCCTTCCCACTCGTGCTGCCCCCG
ACGCGGGAGGTTCACCTCATCCTCTCCTTCGACTTCAGTGCCGGAGATCCTTTCGAGACC
ATCCGGGCTACCACTGACTACTGCCGCCGCCACAAGATCCCCTTTCCCCAAGTAGAAGAG
GCTGAGCTGGATTTGTGGTCCAAGGCCCCCGCCAGCTGCTACATCCTGAAAGGAGAAACT
GGACCAGTGGTGATACATTTTCCCCTGTTCAACATAGATGCCTGTGGAGGTGATATTGAG
GCATGGAGTGACACATACGACACATTCAAGCTTGCTGACACCTACACTCTAGATGTGGTG
GTGCTACTCTTGGCATTAGCCAAGAAGAATGTCAGGGAAAACAAGAAGAAGATCCTTAGA
GAGTTGATGAACGTGGCCGGGCTCTACTACCCGAAGGATAGTGCCCGAAGTTGCTGCTTG
GCATAG
Enzyme 26 GenBank Gene ID AF058921 Link Image
Enzyme 26 GeneCard ID PLA2G4C Link Image
Enzyme 26 GenAtlas ID PLA2G4C Link Image
Enzyme 26 HGNC ID HGNC:9037 Link Image
Enzyme 26 Chromosome Location 19
Enzyme 26 Locus 19q13.3
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Underwood KW, Song C, Kriz RW, Chang XJ, Knopf JL, Lin LL: A novel calcium-independent phospholipase A2, cPLA2-gamma, that is prenylated and contains homology to cPLA2. J Biol Chem. 1998 Aug 21;273(34):21926-32. [PubMed Link Image]
  2. Pickard RT, Strifler BA, Kramer RM, Sharp JD: Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1999 Mar 26;274(13):8823-31. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5781
Enzyme 27 Name Hormone-sensitive lipase
Enzyme 27 Synonyms
  1. HSL
Enzyme 27 Gene Name LIPE
Enzyme 27 Protein Sequence >Hormone-sensitive lipase
MEPGSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPLTQ
QETPAQHDAESQKEPRAQQKSASQEEFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLG
KESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQET
PEQSDKQTTPVQGAKSKQGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVGS
SSDTDSPATMGGMVAQGVKLGFKGKSGYKVMSGYSGTSPHEKTSARNHRHYQDTASRLIH
NMDLRTMTQSLVTLAEDNIAFFSSQGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAH
LFDLDPETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALT
QLRALVYYAQRLLVTNRPGVLFFEGDEGLTADFLREYVTLHKGCFYGRCLGFQFTPAIRP
FLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWK
AFWNITEMEVLSSLANMASATVRVSRLLSLPPEAFEMPLTADPTLTVTISPPLAHTGPGP
VLVRLISYDLREGQDSEELSSLIKSNGQRSLELWPRPQQAPRSRSLIVHFHGGGFVAQTS
RSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERIC
LAGDSAGGNLCFTVALRAAAYGVRVPDGIMAAYPATMLQPAASPSRLLSLMDPLLPLSVL
SKCVSAYAGAKTEDHSNSDQKALGMMGLVRRDTALLLRDFRLGASSWLNSFLELSGRKSQ
KMSEPIAEPMRRSVSEAALAQPQGPLGTDSLKNLTLRDLSLRGNSETSSDTPEMSLSAET
LSPSTPSDVNFLLPPEDAGEEAEAKNELSPMDRGLGVRAAFPEGFHPRRSSQGATQMPLY
SSPIVKNPFMSPLLAPDSMLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVE
DLPHGFLTLAALCRETRQAAELCVERIRLVLTPPAGAGPSGETGAAGVDGGCGGRH
Enzyme 27 Number of Residues 1076
Enzyme 27 Molecular Weight 116599
Enzyme 27 Theoretical pI 6.68
Enzyme 27 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • cholesterol metabolism
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • sterol metabolism
Component
Enzyme 27 General Function Lipid transport and metabolism
Enzyme 27 Specific Function In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions
  • (1) diacylglycerol + H2O = monoacylglycerol + a carboxylate
  • (2) triacylglycerol + H2O = diacylglycerol + a carboxylate
  • (3) monoacylglycerol + H2O = glycerol + a carboxylate
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 896476 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q05469 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name LIPS_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >2328 bp
ATGGACCTGCGCACAATGACACAGTCGCTGGTGACTCTGGCGGAGGACAACATAGCCTTC
TTCTCGAGCCAGGGTCCTGGGGAAACGGCCCAGCGGCTGTCAGGCGTTTTTGCCGGTGTA
CGGGAGCAGGCGCTGGGGCTGGAGCCGGCCCTGGGCCGCCTGCTGGGTGTGGCGCACCTC
TTTGACCTGGACCCAGAGACACCGGCCAACGGGTACCGCAGCCTAGTGCACACAGCCCGC
TGCTGCCTGGCGCACCTCCTGCACAAATCCCGCTATGTGGCCTCCAACCGCCGCAGCATC
TTCTTCCGCACCAGCCACAACCTGGCCGAGCTGGAGGCCTACCTGGCTGCCCTCACCCAG
CTCCGCGCTCTGGTCTACTACGCCCAGCGCCTGCTGGTTACCAATCGGCCGGGGGTACTC
TTCTTTGAGGGCGACGAGGGGCTCACCGCCGACTTCCTCCGGGAGTATGTCACGCTGCAT
AAGGGATGCTTCTATGGCCGCTGCCTGGGCTTCCAGTTCACGCCTGCCATCCGGCCATTC
CTGCAGACCATCTCCATTGGGCTGGTGTCCTTCGGGGAGCACTACAAACGCAACGAGACA
GGCCTCAGTGTGGCCGCCAGCTCTCTCTTCACCAGCGGCCGCTTTGCCATCGACCCCGAG
CTGCGTGGGGCTGAGTTTGAGCGGATCACACAGAACCTGGACGTGCACTTCTGGAAAGCC
TTCTGGAACATCACCGAGATGGAAGTGCTATCGTCTCTGGCCAACATGGCATCGGCCACC
GTGAGGGTAAGCCGCCTGCTCAGCCTGCCACCCGAAGCCTTTGAGATGCCACTGACTGCC
GACCCCACGCTCACGGTCACCATCTCACCCCCACTGGCCCACACAGGCCCTGGGCCCGTC
CTCGTCAGGCTCATCTCCTATGACCTGCGTGAAGGACAGGACAGTGAGGAGCTCAGCAGC
CTGATAAAGTCCAACGGCCAACGGAGCCTGGAGCTGTGGCCGCGCCCCCAGCAGGCACCC
CGCTCGCGGTCCCTGATAGTGCACTTCCACGGCGGTGGCTTTGTGGCCCAGACCTCCAGA
TCCCACGAGCCCTACCTCAAGAGCTGGGCCCAGGAGCTGGGCGCCCCCATCATCTCCATC
GACTACTCCCTGGCCCCTGAGGCCCCCTTCCCCCGTGCGCTGGAGGAGTGCTTCTTCGCC
TACTGCTGGGCCATCAAGCACTGCGCCCTCCTTGGCTCAACAGGGGAACGAATCTGCCTT
GCGGGGGACAGTGCAGGCGGGAACCTCTGCTTCACCGTGGCTCTTCGGGCAGCAGCCTAC
GGGGTGCGGGTGCCAGATGGCATCATGGCAGCCTACCCGGCCACAATGCTGCAGCCTGCC
GCCTCTCCCTCCCGCCTGCTGAGCCTCATGGACCCCTTGCTGCCCCTCAGTGTGCTCTCC
AAGTGTGTCAGCGCCTATGCTGGTGCAAAGACGGAGGACCACTCCAACTCAGACCAGAAA
GCCCTCGGCATGATGGGGCTGGTGCGGCGGGACACAGCCCTGCTCCTCCGAGACTTCCGC
CTGGGTGCCTCCTCATGGCTCAACTCCTTCCTGGAGTTAAGTGGGCGCAAGTCCCAGAAG
ATGTCGGAGCCCATAGCAGAGCCGATGCGCCGCAGTGTGTCTGAAGCAGCACTGGCCCAG
CCCCAGGGCCCACTGGGCACGGATTCCCTCAAGAACCTGACCCTGAGGGACTTGAGCCTG
AGGGGAAACTCCGAGACGTCGTCGGACACCCCCGAGATGTCGCTGTCAGCTGAGACACTT
AGCCCCTCCACACCCTCCGATGTCAACTTCTTATTACCACCTGAGGATGCAGGGGAAGAG
GCTGAGGCCAAAAATGAGCTGAGCCCCATGGACAGAGGCCTGGGCGTCCGTGCCGCCTTC
CCCGAGGGTTTCCACCCCCGACGCTCCAGCCAGGGTGCCACACAGATGCCCCTCTACTCC
TCACCCATAGTCAAGAACCCCTTCATGTCGCCGCTGCTGGCACCCGACAGCATGCTCAAG
AGCCTGCCACCTGTGCACATCGTGGCGTGCGCGCTGGACCCCATGCTGGACGACTCGGTC
ATGCTCGCGCGGCGACTGCGCAACCTGGGCCAGCCGGTGACGCTGCGCGTGGTGGAGGAC
CTGCCGCACGGCTTCCTGACCCTAGCGGCGCTGTGCCGCGAGACGCGCCAGGCCGCAGAG
CTGTGCGTGGAGCGCATCCGCCTCGTCCTCACTCCTCCCGCCGGAGCCGGGCCGAGCGGG
GAGACGGGGGCTGCGGGGGTAGACGGGGGCTGCGGGGGGCGACACTAA
Enzyme 27 GenBank Gene ID L11706 Link Image
Enzyme 27 GeneCard ID LIPE Link Image
Enzyme 27 GenAtlas ID LIPE Link Image
Enzyme 27 HGNC ID HGNC:6621 Link Image
Enzyme 27 Chromosome Location 19
Enzyme 27 Locus 19q13.2
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Langin D, Laurell H, Holst LS, Belfrage P, Holm C: Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4897-901. [PubMed Link Image]
  2. Holst LS, Langin D, Mulder H, Laurell H, Grober J, Bergh A, Mohrenweiser HW, Edgren G, Holm C: Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase. Genomics. 1996 Aug 1;35(3):441-7. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5783
Enzyme 28 Name Group 3 secretory phospholipase A2 precursor
Enzyme 28 Synonyms
  1. Group III secretory phospholipase A2
  2. Phosphatidylcholine 2-acylhydrolase GIII
  3. GIII sPLA2
Enzyme 28 Gene Name PLA2G3
Enzyme 28 Protein Sequence >Group 3 secretory phospholipase A2 precursor
MGVQAGLFGMLGFLGVALGGSPALRWYRTSCHLTKAVPGNPLGYLSFLAKDAQGLALIHA
RWDAHRRLQACSWEDEPELTAAYGALCAHETAWGSFIHTPGPELQRALATLQSQWEACRA
LEESPAGARKKRAAGQSGVPGGGHQREKRGWTMPGTLWCGVGDSAGNSSELGVFQGPDLC
CREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDIVGVAFFNVL
EIPCFVLEEQEACVAWYWWGGCRMYGTVPLARLQPRTFYNASWSSRATSPTPSSRSPAPP
KPRQKQHLRKGPPHQKGSKRPSKANTTALQDPMVSPRLDVAPTGLQGPQGGLKPQGARWV
CRSFRRHLDQCEHQIGPREIEFQLLNSAQEPLFHCNCTRRLARFLRLHSPPEVTNMLWEL
LGTTCFKLAPPLDCVEGKNCSRDPRAIRVSARHLRRLQQRRHQLQDKGTDERQPWPSEPL
RGPMSFYNQCLQLTQAARRPDRQQKSWSQ
Enzyme 28 Number of Residues 509
Enzyme 28 Molecular Weight 57152
Enzyme 28 Theoretical pI 9.23
Enzyme 28 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • cellular lipid metabolism
  • lipid catabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • extracellular region
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Shows an 11-fold preference for phosphatidylglycerol over phosphatidylcholine
Enzyme 28 Pathways
Enzyme 28 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • 1-19
Enzyme 28 Transmembrane Regions Not Available
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 7274380 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q9NZ20 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name PA2G3_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1530 bp
ATGGGGGTTCAGGCAGGGCTGTTTGGGATGCTGGGCTTCCTGGGGGTGGCCCTGGGGGGC
TCCCCTGCCCTCCGCTGGTACAGGACCTCCTGCCACTTGACCAAGGCCGTCCCTGGCAAC
CCACTGGGGTACCTGAGCTTCCTGGCCAAGGATGCTCAGGGACTGGCCCTGATCCATGCC
CGCTGGGATGCGCATAGGAGGCTGCAGGCATGTAGCTGGGAGGATGAGCCGGAGCTCACC
GCAGCCTACGGTGCTCTCTGTGCTCATGAGACTGCCTGGGGCTCCTTCATCCACACCCCC
GGACCCGAGCTGCAGAGAGCACTGGCCACTCTTCAGAGTCAGTGGGAGGCATGCCGAGCG
CTTGAGGAGAGTCCAGCAGGGGCCAGGAAGAAGCGAGCAGCAGGGCAGAGTGGAGTCCCT
GGTGGAGGGCACCAGCGAGAGAAGAGAGGATGGACCATGCCTGGCACACTGTGGTGTGGA
GTTGGAGATTCTGCTGGGAACTCCTCGGAGCTGGGGGTCTTCCAGGGACCTGATCTCTGT
TGCCGGGAACATGACCGCTGCCCACAGAACATCTCACCCTTGCAGTACAACTATGGCATC
CGAAACTACCGATTCCACACCATCTCCCACTGTGACTGTGACACCAGGTTTCAGCAATGC
CTACAGAATCAGCACGACTCCATCTCGGACATCGTGGGCGTGGCCTTCTTCAACGTGCTG
GAGATCCCCTGCTTTGTGCTGGAGGAGCAGGAGGCGTGTGTGGCGTGGTACTGGTGGGGC
GGGTGTAGGATGTACGGCACAGTGCCCCTCGCTCGCCTGCAGCCCAGGACCTTCTACAAT
GCCTCCTGGAGCTCCCGGGCCACCTCCCCAACTCCCAGCTCCCGGAGCCCAGCCCCTCCC
AAGCCTCGACAGAAGCAGCACCTTCGGAAGGGGCCACCACATCAGAAAGGGTCCAAGCGC
CCCAGCAAAGCCAACACCACAGCCCTCCAGGACCCTATGGTCTCTCCCAGGCTTGATGTG
GCCCCCACAGGCCTCCAGGGCCCACAGGGTGGCCTAAAACCTCAGGGTGCCCGCTGGGTC
TGCCGCAGCTTCCGCCGCCACCTGGACCAGTGTGAGCACCAGATTGGGCCCCGGGAAATC
GAGTTCCAGCTGCTCAACAGCGCCCAAGAGCCCCTCTTCCACTGCAACTGCACGCGCCGT
CTGGCACGCTTCCTGAGGCTCCACAGCCCACCCGAGGTTACCAACATGCTTTGGGAGCTG
CTGGGCACAACCTGCTTCAAGCTGGCCCCTCCACTGGACTGTGTGGAAGGCAAAAACTGT
TCCAGAGACCCTAGGGCCATCAGGGTGTCAGCCCGGCACTTGCGGAGGCTTCAGCAGAGG
CGACACCAGCTCCAGGATAAAGGCACAGATGAGAGGCAGCCATGGCCTTCAGAGCCCCTG
AGAGGCCCCATGTCATTCTACAACCAGTGCCTGCAGCTAACCCAGGCAGCCAGGAGACCC
GACAGGCAGCAGAAGTCCTGGAGCCAGTGA
Enzyme 28 GenBank Gene ID AF220490 Link Image
Enzyme 28 GeneCard ID PLA2G3 Link Image
Enzyme 28 GenAtlas ID PLA2G3 Link Image
Enzyme 28 HGNC ID HGNC:17934 Link Image
Enzyme 28 Chromosome Location 22
Enzyme 28 Locus 22q11.2-q13.2
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Valentin E, Ghomashchi F, Gelb MH, Lazdunski M, Lambeau G: Novel human secreted phospholipase A(2) with homology to the group III bee venom enzyme. J Biol Chem. 2000 Mar 17;275(11):7492-6. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 5821
Enzyme 29 Name Bile acid CoA:amino acid N-acyltransferase
Enzyme 29 Synonyms
  1. BAT
  2. BACAT
  3. Glycine N-choloyltransferase
  4. Long-chain fatty-acyl-CoA hydrolase
Enzyme 29 Gene Name BAAT
Enzyme 29 Protein Sequence >Bile acid CoA:amino acid N-acyltransferase
MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDL
NHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVAS
APKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASL
LASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQI
GLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFE
TTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGA
GHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL
Enzyme 29 Number of Residues 418
Enzyme 29 Molecular Weight 46300
Enzyme 29 Theoretical pI 7.00
Enzyme 29 GO Classification
Function
  • CoA hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 29 General Function Not Available
Enzyme 29 Specific Function Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs
Enzyme 29 Pathways
Enzyme 29 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 532505 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q14032 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name BAAT_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1257 bp
ATGATCCAGTTGACAGCTACCCCTGTGAGTGCACTTGTTGATGAGCCAGTGCATATCCGA
GCTACAGGCCTGATTCCCTTTCAGATGGTGAGTTTTCAGGCATCACTGGAAGATGAAAAC
GGAGACATGTTTTATTCTCAAGCCCACTATAGGGCCAATGAATTCGGTGAGGTGGACCTG
AATCATGCTTCTTCACTTGGAGGGGATTATATGGGAGTCCACCCCATGGGTCTCTTCTGG
TCTCTGAAACCTGAAAAGCTATTAACAAGACTGTTGAAAAGAGATGTGATGAATAGGCCT
TTCCAGGTCCAAGTAAAACTTTATGACTTAGAGTTAATAGTGAACAATAAAGTTGCCAGT
GCTCCAAAGGCCAGCCTGACTTTGGAGAGGTGGTATGTGGCACCTGGTGTCACACGAATT
AAGGTTCGAGAAGGCCGCCTTCGAGGAGCTCTCTTTCTCCCTCCAGGAGAGGGTCTCTTC
CCAGGGGTAATTGATTTGTTTGGTGGTTTGGGTGGGCTGCTTGAATTTCGGGCCAGCCTC
CTAGCCAGTCGTGGCTTCGCCTCCTTGGCCTTGGCTTACCATAACTATGAAGACCTGCCC
CGCAAACCAGAAGTAACAGATTTGGAATATTTTGAGGAGGCTGCCAACTTTCTCCTGAGA
CATCCAAAGGTCTTTGGCTCAGGCGTTGGGGTAGTCTCTGTATGTCAAGGAGTACAGATT
GGACTATCTATGGCTATTTACCTAAAGCAAGTCACAGCCACGGTACTTATTAATGGGACC
AACTTTCCTTTTGGCATTCCACAGGTATATCATGGTCAGATCCATCAGCCCCTTCCCCAT
TCTGCACAATTAATATCCACCAATGCCTTGGGGTTACTAGAGCTCTATCGCACTTTTGAG
ACAACTCAAGTTGGGGCCAGTCAATATTTGTTTCCTATTGAAGAGGCCCAGGGGCAATTC
CTCTTCATTGTAGGAGAAGGTGATAAGACTATCAACAGCAAAGCACACGCTGAACAAGCC
ATAGGACAGCTGAAGAGACATGGGAAGAACAACTGGACCCTGCTATCTTACCCTGGGGCA
GGCCACCTGATAGAACCTCCCTATTCTCCTCTGTGCTGTGCCTCAACGACCCACGATTTG
AGGTTACACTGGGGAGGAGAGGTGATCCCACACGCAGCTGCACAGGAACATGCTTGGAAG
GAGATCCAGAGATTTCTCAGGAAGCACCTCATTCCAGATGTGACCAGTCAACTCTAA
Enzyme 29 GenBank Gene ID L34081 Link Image
Enzyme 29 GeneCard ID BAAT Link Image
Enzyme 29 GenAtlas ID BAAT Link Image
Enzyme 29 HGNC ID HGNC:932 Link Image
Enzyme 29 Chromosome Location 9
Enzyme 29 Locus 9q22.3
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Falany CN, Johnson MR, Barnes S, Diasio RB: Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase. J Biol Chem. 1994 Jul 29;269(30):19375-9. [PubMed Link Image]
  2. Carlton VE, Harris BZ, Puffenberger EG, Batta AK, Knisely AS, Robinson DL, Strauss KA, Shneider BL, Lim WA, Salen G, Morton DH, Bull LN: Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat Genet. 2003 May;34(1):91-6. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 5824
Enzyme 30 Name Acylphosphatase-2
Enzyme 30 Synonyms
  1. Acylphosphate phosphohydrolase 2
  2. Acylphosphatase, muscle type isozyme
Enzyme 30 Gene Name ACYP2
Enzyme 30 Protein Sequence >Acylphosphatase-2
MSTAQSLKSVDYEVFGRVQGVCFRMYTEDEARKIGVVGWVKNTSKGTVTGQVQGPEDKVN
SMKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSNFSIRY
Enzyme 30 Number of Residues 99
Enzyme 30 Molecular Weight 11140
Enzyme 30 Theoretical pI 10.01
Enzyme 30 GO Classification
Function
  • acylphosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
Process
Component
Enzyme 30 General Function Energy production and conversion
Enzyme 30 Specific Function Its physiological role is not yet clear
Enzyme 30 Pathways
Enzyme 30 Reactions
  • An acylphosphate + H2O = a carboxylate + phosphate
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 15341747 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID P14621 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name ACYP2_HUMAN Link Image
Enzyme 30 PDB ID 1APS Link Image
Enzyme 30 PDB File Show
Enzyme 30 3D Structure
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >300 bp
ATGTCTACCGCCCAGTCACTCAAATCCGTGGACTACGAGGTGTTCGGAAGAGTGCAGGGT
GTTTGCTTCAGAATGTATACAGAAGATGAAGCTAGGAAAATAGGAGTGGTTGGCTGGGTG
AAGAATACCAGCAAAGGCACCGTGACAGGCCAAGTGCAGGGGCCAGAAGACAAAGTCAAT
TCCATGAAGTCCTGGCTGAGCAAGGTTGGAAGCCCTAGTTCTCGCATTGACCGCACAAAC
TTTTCTAATGAAAAAACCATCTCTAAGCTTGAATACTCTAATTTTAGTATTAGATACTAA
Enzyme 30 GenBank Gene ID BC012290 Link Image
Enzyme 30 GeneCard ID ACYP2 Link Image
Enzyme 30 GenAtlas ID ACYP2 Link Image
Enzyme 30 HGNC ID HGNC:180 Link Image
Enzyme 30 Chromosome Location 2
Enzyme 30 Locus 2p16.2
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Manao G, Camici G, Modesti A, Liguri G, Berti A, Stefani M, Cappugi G, Ramponi G: Human skeletal muscle acylphosphatase: the primary structure. Mol Biol Med. 1984 Dec;2(6):369-78. [PubMed Link Image]
  2. Chiarugi P, Raugei G, Marzocchini R, Fiaschi T, Ciccarelli C, Berti A, Ramponi G: Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone. Biochem J. 1995 Oct 15;311 ( Pt 2):567-73. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 5825
Enzyme 31 Name Acylphosphatase-1
Enzyme 31 Synonyms
  1. Acylphosphate phosphohydrolase 1
  2. Acylphosphatase, organ-common type isozyme
  3. Acylphosphatase, erythrocyte isozyme
Enzyme 31 Gene Name ACYP1
Enzyme 31 Protein Sequence >Acylphosphatase-1
MAEGNTLISVDYEIFGKVQGVFFRKHTQAEGKKLGLVGWVQNTDRGTVQGQLQGPISKVR
HMQEWLETRGSPKSHIDKANFNNEKVILKLDYSDFQIVK
Enzyme 31 Number of Residues 99
Enzyme 31 Molecular Weight 11261
Enzyme 31 Theoretical pI 9.94
Enzyme 31 GO Classification
Function
  • acylphosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
Process
Component
Enzyme 31 General Function Energy production and conversion
Enzyme 31 Specific Function Its physiological role is not yet clear
Enzyme 31 Pathways
Enzyme 31 Reactions
  • An acylphosphate + H2O = a carboxylate + phosphate
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 1834464 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID P07311 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name ACYP1_HUMAN Link Image
Enzyme 31 PDB ID 2ACY Link Image
Enzyme 31 PDB File Show
Enzyme 31 3D Structure
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >300 bp
ATGGCAGAGGGAAACACCCTGATATCAGTGGATTATGAAATTTTTGGGAAGGTGCAAGGG
GTGTTTTTCCGTAAGCATACTCAGGCTGAGGGTAAAAAGCTGGGATTGGTAGGCTGGGTC
CAGAACACTGACCGGGGCACAGTGCAAGGACAATTGCAAGGTCCAATCTCCAAGGTGCGT
CATATGCAGGAATGGCTTGAAACAAGAGGAAGTCCTAAATCACACATCGACAAAGCAAAC
TTCAACAATGAAAAAGTCATCTTGAAGTTGGATTACTCAGACTTCCAAATTGTAAAATAA
Enzyme 31 GenBank Gene ID X84194 Link Image
Enzyme 31 GeneCard ID ACYP1 Link Image
Enzyme 31 GenAtlas ID ACYP1 Link Image
Enzyme 31 HGNC ID HGNC:179 Link Image
Enzyme 31 Chromosome Location 14
Enzyme 31 Locus 14q24.3
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  2. Liguri G, Camici G, Manao G, Cappugi G, Nassi P, Modesti A, Ramponi G: A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure. Biochemistry. 1986 Dec 2;25(24):8089-94. [PubMed Link Image]
  3. Fiaschi T, Raugei G, Marzocchini R, Chiarugi P, Cirri P, Ramponi G: Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase. FEBS Lett. 1995 Jun 26;367(2):145-8. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 5826
Enzyme 32 Name Aminoacylase-1
Enzyme 32 Synonyms
  1. N-acyl-L-amino-acid amidohydrolase
  2. ACY-1
Enzyme 32 Gene Name ACY1
Enzyme 32 Protein Sequence >Aminoacylase-1
MTSKGPEEEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVV
TVLTWPGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQ
YLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALRAGFALDEGIANP
TDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSN
PHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEG
VTLEFAQKWMHPQVTPTDDSNPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPAL
GFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALASVPALPSDS
Enzyme 32 Number of Residues 408
Enzyme 32 Molecular Weight 45885
Enzyme 32 Theoretical pI 6.12
Enzyme 32 GO Classification
Function
  • aminoacylase activity
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
  • metallopeptidase activity
  • peptidase activity
  • protein binding
  • protein dimerization activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • cellular protein metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
  • proteolysis
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 32 General Function Amino acid transport and metabolism
Enzyme 32 Specific Function Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate)
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions
  • An N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 178071 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q03154 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name ACY1_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1227 bp
ATGACCAGCAAGGGTCCCGAGGAGGAGCACCCATCGGTGACGCTCTTCCGCCAGTACCTG
CGTATCCGCACTGTCCAGCCCAAGCCTGACTATGGAGCTGCTGTGGCTTTCTTTGAGGAG
ACAGCCCGCCAGCTGGGCCTGGGCTGTCAGAAAGTAGAGGTGGCACCTGGCTATGTGGTG
ACCGTGTTGACCTGGCCAGGCACCAACCCTACACTCTCCTCCATCTTGCTCAACTCCCAC
ACGGATGTGGTGCCTGTCTTCAAGGAACATTGGAGTCACGACCCCTTTGAGGCCTTCAAG
GATTCTGAGGGCTACATCTATGCCAGGGGTGCCCAGGACATGAAGTGCGTCAGCATCCAG
TACCTGGAAGCTGTGAGGAGGCTGAAGGTGGAGGGCCACCGGTTCCCCAGAACCATCCAC
ATGACCTTTGTGCCTGATGAGGAGGTTGGGGGTCACCAAGGCATGGAGCTGTTCGTGCAG
CGGCCTGAGTTCCACGCCCTGAGGGCAGGCTTTGCCCTGGATGAGGGCATAGCCAATCCC
ACTGATGCCTTCACTGTCTTTTATAGTGAGCGGAGTCCCTGGTGGGTGCGGGTTACCAGC
ACTGGGAGGCCAGGCCATGCCTCACGCTTCATGGAGGACACAGCAGCAGAGAAGCTGCAC
AAGGTTGTAAACTCCATCCTGGCATTCCGGGAGAAGGAATGGCAGAGGCTGCAGTCAAAC
CCCCACCTGAAAGAGGGGTCCGTGACCTCCGTGAACCTGACTAAGCTAGAGGGTGGCGTG
GCCTATAACGTGATACCTGCCACCATGAGCGCCAGCTTTGACTTCCGTGTGGCACCGGAT
GTGGACTTCAAGGCTTTTGAGGAGCAGCTGCAGAGCTGGTGCCAGGCAGCTGGCGAGGGG
GTCACCCTAGAGTTTGCTCAGAAGTGGATGCACCCCCAAGTGACACCTACTGATGACTCA
AACCCTTGGTGGGCAGCTTTTAGCCGGGTCTGCAAGGATATGAACCTCACTCTGGAGCCT
GAGATCATGCCTGCTGCCACTGACAACCGCTATATCCGCGCGGTGGGGGTCCCAGCTCTA
GGCTTCTCACCCATGAACCGCACACCTGTGCTGCTGCACGACCACGATGAACGGCTGCAT
GAGGCTGTGTTCCTCCGTGGGGTGGACATATATACACGCCTGCTGCCTGCCCTTGCCAGT
GTGCCTGCCCTGCCCAGTGACAGCTGA
Enzyme 32 GenBank Gene ID L07548 Link Image
Enzyme 32 GeneCard ID ACY1 Link Image
Enzyme 32 GenAtlas ID ACY1 Link Image
Enzyme 32 HGNC ID HGNC:177 Link Image
Enzyme 32 Chromosome Location 3
Enzyme 32 Locus 3p21.1
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Mitta M, Kato I, Tsunasawa S: The nucleotide sequence of human aminoacylase-1. Biochim Biophys Acta. 1993 Aug 19;1174(2):201-3. [PubMed Link Image]
  2. Cook RM, Burke BJ, Buchhagen DL, Minna JD, Miller YE: Human aminoacylase-1. Cloning, sequence, and expression analysis of a chromosome 3p21 gene inactivated in small cell lung cancer. J Biol Chem. 1993 Aug 15;268(23):17010-7. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 5827
Enzyme 33 Name Aspartoacylase
Enzyme 33 Synonyms
  1. Aminoacylase-2
  2. ACY-2
Enzyme 33 Gene Name ASPA
Enzyme 33 Protein Sequence >Aspartoacylase
MTSCHIAEEHIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAVKK
CTRYIDCDLNRIFDLENLGKKMSEDLPYEVRRAQEINHLFGPKDSEDSYDIIFDLHNTTS
NMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIEHPSLKYATTRSIAKYPVGIEVG
PQPQGVLRADILDQMRKMIKHALDFIHHFNEGKEFPPCAIEVYKIIEKVDYPRDENGEIA
AIIHPNLQDQDWKPLHPGDPMFLTLDGKTIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTK
LTLNAKSIRCCLH
Enzyme 33 Number of Residues 313
Enzyme 33 Molecular Weight 35736
Enzyme 33 Theoretical pI 6.51
Enzyme 33 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • metabolism
  • physiological process
Component
Enzyme 33 General Function Amino acid transport and metabolism
Enzyme 33 Specific Function Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it act as a scavenger of NAA from body fluids
Enzyme 33 Pathways
Enzyme 33 Reactions
  • N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 455834 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID P45381 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name ACY2_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >942 bp
ATGACTTCTTGTCACATTGCTGAAGAACATATACAAAAGGTTGCTATCTTTGGAGGAACC
CATGGGAATGAGCTAACCGGAGTATTTCTGGTTAAGCATTGGCTAGAGAATGGCGCTGAG
ATTCAGAGAACAGGGCTGGAGGTAAAACCATTTATTACTAACCCCAGAGCAGTGAAGAAG
TGTACCAGATATATTGACTGTGACCTGAATCGCATTTTTGACCTTGAAAATCTTGGCAAA
AAAATGTCAGAAGATTTGCCATATGAAGTGAGAAGGGCTCAAGAAATAAATCATTTATTT
GGTCCAAAAGACAGTGAAGATTCCTATGACATTATTTTTGACCTTCACAACACCACCTCT
AACATGGGGTGCACTCTTATTCTTGAGGATTCCAGGAATAACTTTTTAATTCAGATGTTT
CATTACATTAAGACTTCTCTGGCTCCACTACCCTGCTACGTTTATCTGATTGAGCATCCT
TCCCTCAAATATGCGACCACTCGTTCCATAGCCAAGTATCCTGTGGGTATAGAAGTTGGT
CCTCAGCCTCAAGGGGTTCTGAGAGCTGATATCTTGGATCAAATGAGAAAAATGATTAAA
CATGCTCTTGATTTTATACATCATTTCAATGAAGGAAAAGAATTTCCTCCCTGCGCCATT
GAGGTCTATAAAATTATAGAGAAAGTTGATTACCCCCGGGATGAAAATGGAGAAATTGCT
GCTATCATCCATCCTAATCTGCAGGATCAAGACTGGAAACCACTGCATCCTGGGGATCCC
ATGTTTTTAACTCTTGATGGGAAGACGATCCCACTGGGCGGAGACTGTACCGTGTACCCC
GTGTTTGTGAATGAGGCCGCATATTACGAAAAGAAAGAAGCTTTTGCAAAGACAACTAAA
CTAACGCTCAATGCAAAAAGTATTCGCTGCTGTTTACATTAG
Enzyme 33 GenBank Gene ID S67156 Link Image
Enzyme 33 GeneCard ID ASPA Link Image
Enzyme 33 GenAtlas ID ASPA Link Image
Enzyme 33 HGNC ID HGNC:756 Link Image
Enzyme 33 Chromosome Location 17
Enzyme 33 Locus 17pter-p13
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Kaul R, Gao GP, Balamurugan K, Matalon R: Cloning of the human aspartoacylase cDNA and a common missense mutation in Canavan disease. Nat Genet. 1993 Oct;5(2):118-23. [PubMed Link Image]
  2. Moore RA, Le Coq J, Faehnle CR, Viola RE: Purification and preliminary characterization of brain aspartoacylase. Arch Biochem Biophys. 2003 May 1;413(1):1-8. [PubMed Link Image]
  3. Kaul R, Gao GP, Aloya M, Balamurugan K, Petrosky A, Michals K, Matalon R: Canavan disease: mutations among Jewish and non-jewish patients. Am J Hum Genet. 1994 Jul;55(1):34-41. [PubMed Link Image]
  4. Shaag A, Anikster Y, Christensen E, Glustein JZ, Fois A, Michelakakis H, Nigro F, Pronicka E, Ribes A, Zabot MT, et al.: The molecular basis of canavan (aspartoacylase deficiency) disease in European non-Jewish patients. Am J Hum Genet. 1995 Sep;57(3):572-80. [PubMed Link Image]
  5. Kaul R, Gao GP, Michals K, Whelan DT, Levin S, Matalon R: Novel (cys152 > arg) missense mutation in an Arab patient with Canavan disease. Hum Mutat. 1995;5(3):269-71. [PubMed Link Image]
  6. Kobayashi K, Tsujino S, Ezoe T, Hamaguchi H, Nihei K, Sakuragawa N: Missense mutation (I143T) in a Japanese patient with Canavan disease. Hum Mutat. 1998;Suppl 1:S308-9. [PubMed Link Image]
  7. Rady PL, Vargas T, Tyring SK, Matalon R, Langenbeck U: Novel missense mutation (Y231C) in a turkish patient with canavan disease. Am J Med Genet. 1999 Nov 26;87(3):273-5. [PubMed Link Image]
  8. Sistermans EA, de Coo RF, van Beerendonk HM, Poll-The BT, Kleijer WJ, van Oost BA: Mutation detection in the aspartoacylase gene in 17 patients with Canavan disease: four new mutations in the non-Jewish population. Eur J Hum Genet. 2000 Jul;8(7):557-60. [PubMed Link Image]
  9. Zeng BJ, Wang ZH, Ribeiro LA, Leone P, De Gasperi R, Kim SJ, Raghavan S, Ong E, Pastores GM, Kolodny EH: Identification and characterization of novel mutations of the aspartoacylase gene in non-Jewish patients with Canavan disease. J Inherit Metab Dis. 2002 Nov;25(7):557-70. [PubMed Link Image]
  10. Olsen TR, Tranebjaerg L, Kvittingen EA, Hagenfeldt L, Moller C, Nilssen O: Two novel aspartoacylase gene (ASPA) missense mutations specific to Norwegian and Swedish patients with Canavan disease. J Med Genet. 2002 Sep;39(9):e55. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 5830
Enzyme 34 Name Aspartoacylase-2
Enzyme 34 Synonyms
  1. Aminoacylase-3
  2. ACY-3
  3. Acylase III
  4. Hepatitis C virus core-binding protein 1
  5. HCBP1
Enzyme 34 Gene Name ACY3
Enzyme 34 Protein Sequence >Aspartoacylase-2
MCSLPVPREPLRRVAVTGGTHGNEMSGVYLARHWLHAPAELQRASFSAVPVLANPAATSG
CRRYVDHDLNRTFTSSFLNSRPTPDDPYEVTRARELNQLLGPKASGQAFDFVLDLHNTTA
NMGTCLIAKSSHEVFAMHLCRHLQLQYPELSCQVFLYQRSGEESYNLDSVAKNGLGLELG
PQPQGVLRADIFSRMRTLVATVLDFIELFNQGTAFPAFEMEAYRPVGVVDFPRTEAGHLA
GTVHPQLQDRDFQPLQPGAPIFQMFSGEDLLYEGESTVYPVFINEAAYYEKGVAFVQTEK
FTFTVPAMPALTPAPSPAS
Enzyme 34 Number of Residues 319
Enzyme 34 Molecular Weight 35241
Enzyme 34 Theoretical pI 5.77
Enzyme 34 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • metabolism
  • physiological process
Component
Enzyme 34 General Function Amino acid transport and metabolism
Enzyme 34 Specific Function N-acyl-L-aspartate + H(2)O = a carboxylate + L-aspartate
Enzyme 34 Pathways
Enzyme 34 Reactions
  • N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 21654856 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q96HD9 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name ACY3_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >960 bp
ATGTGCTCACTGCCTGTGCCCCGGGAGCCCCTGCGTCGCGTGGCTGTGACTGGGGGCACG
CATGGCAACGAGATGTCGGGCGTCTACCTGGCCCGGCACTGGCTGCATGCCCCCGCAGAG
CTGCAGAGAGCCAGCTTCTCCGCTGTGCCTGTGCTGGCCAACCCGGCAGCCACATCCGGC
TGCCGCCGCTACGTGGACCATGACCTCAACCGCACCTTCACCAGCAGCTTCCTCAATTCC
AGGCCCACCCCGGACGACCCATATGAGGTGACAAGAGCCCGAGAGCTGAACCAGCTGCTG
GGGCCCAAGGCCTCGGGCCAGGCCTTTGACTTTGTCCTTGACCTGCACAACACCACGGCC
AACATGGGCACCTGCTTAATCGCGAAGTCCTCCCACGAAGTCTTTGCCATGCACCTGTGC
CGCCATCTGCAGCTGCAGTACCCCGAGCTGTCCTGCCAGGTCTTCCTGTACCAGCGGTCT
GGGGAGGAGAGCTACAACCTGGACTCTGTGGCCAAAAATGGACTGGGTCTGGAGCTGGGC
CCCCAGCCACAGGGTGTGCTGCGGGCTGACATTTTCTCAAGGATGAGGACCCTGGTGGCC
ACAGTTCTGGACTTCATCGAACTCTTCAACCAGGGTACGGCCTTTCCTGCCTTTGAGATG
GAAGCCTATAGACCCGTGGGCGTCGTGGACTTCCCCCGCACCGAGGCCGGGCACCTGGCA
GGCACTGTGCATCCTCAGCTGCAGGACCGAGACTTCCAGCCACTGCAGCCTGGTGCTCCC
ATCTTCCAGATGTTCAGTGGGGAGGACCTGCTCTATGAGGGAGAGTCCACGGTGTACCCC
GTGTTCATTAACGAGGCTGCCTACTATGAGAAGGGCGTTGCCTTTGTCCAGACTGAGAAG
TTCACATTCACCGTGCCTGCCATGCCCGCGCTGACCCCTGCCCCGAGCCCAGCTTCCTAA
Enzyme 34 GenBank Gene ID AY040761 Link Image
Enzyme 34 GeneCard ID ACY3 Link Image
Enzyme 34 GenAtlas ID ACY3 Link Image
Enzyme 34 HGNC ID HGNC:24104 Link Image
Enzyme 34 Chromosome Location 11
Enzyme 34 Locus 11q13.2
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References Not Available
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 5842
Enzyme 35 Name Long-chain-fatty-acid--CoA ligase 4
Enzyme 35 Synonyms
  1. Long-chain acyl-CoA synthetase 4
  2. LACS 4
Enzyme 35 Gene Name ACSL4
Enzyme 35 Protein Sequence >Long-chain-fatty-acid--CoA ligase 4
MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYR
SVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLIL
GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTL
YATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPE
GFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT
GQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSK
GDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLC
NLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEV
TDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAED
YSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDN
ICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAM
KLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMYGGK
Enzyme 35 Number of Residues 711
Enzyme 35 Molecular Weight 79189
Enzyme 35 Theoretical pI 8.51
Enzyme 35 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 35 General Function Lipid transport and metabolism
Enzyme 35 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arachidonate and eicosapentaenoate as substrates
Enzyme 35 Pathways
Enzyme 35 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • 1-23
Enzyme 35 Transmembrane Regions Not Available
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 3158351 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID O60488 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name ACSL4_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >2013 bp
ATGGCAAAGAGAATAAAAGCTAAGCCCACTTCAGACAAACCTGGAAGTCCATATCGCTCT
GTCACACACTTCGACTCACTAGCTGTAATAGACATCCCTGGAGCAGATACTCTGGATAAA
TTATTTGACCATGCTGTATCCAAGTTTGGGAAGAAGGACAGCCTTGGGACCAGGGAAATC
CTAAGTGAAGAAAATGAAATGCAGCCAAATGGAAAAGTTTTTAAGAAGTTAATTCTTGGG
AATTATAAATGGATGAACTATCTTGAAGTGAATCGCAGAGTGAATAACTTTGGTAGTGGA
CTCACTGCACTGGGACTAAAACCAAAGAACACCATTGCCATCTTCTGTGAGACCAGGGCC
GAATGGATGATTGCAGCACAGACCTGCTTTAAGTACAACTTTCCTCTTGTGACTTTATAT
GCCACACTTGGCAAAGAAGCAGTAGTTCATGGGCTAAATGAATCTGAGGCTTCCTATCTG
ATTACCAGTGTTGAACTTCTGGAAAGTAAACTTAAGACTGCATTGTTAGATATCAGTTGT
GTTAAACATATCATTTATGTGGACAATAAGGCTATCAATAAAGCAGAGTACCCTGAAGGA
TTTGAGATTCACAGCATGCAATCAGTAGAAGAGTTGGGATCTAACCCAGAAAACTTGGGC
ATTCCTCCAAGTAGACCAACGCCTTCAGACATGGCCATTGTTATGTATACTAGTGGTTCT
ACTGGCCGACCTAAGGGAGTGATGATGCATCATAGCAATTTGATAGCTGGAATGACAGGC
CAGTGTGAAAGAATACCTGGACTGGGACCGAAGGACACATATATTGGCTACTTGCCTTTG
GCTCATGTGCTAGAACTGACAGCAGAGATATCTTGCTTTACCTATGGCTGCAGGATTGGA
TATTCTTCTCCGCTTACACTCTCTGACCAGTCCAGCAAAATTAAAAAAGGAAGCAAAGGA
GACTGTACTGTACTGAAGCCCACACTTATGGCTGCTGTTCCGGAAATCATGGATAGAATT
TATAAGAATGTTATGAGCAAAGTCCAAGAGATGAATTATATTCAGAAAACTCTGTTCAAG
ATAGGGTATGATTACAAATTGGAACAGATCAAAAAGGGATATGATGCACCTCTTTGCAAT
CTGTTACTGTTTAAAAAGGTCAAGGCCCTGCTGGGAGGGAATGTCCGCATGATGCTGTCT
GGAGGGGCCCCGCTATCTCCTCAGACACACCGATTCATGAATGTCTGCTTCTGCTGCCCA
ATTGGCCAGGGTTATGGACTGACAGAATCATGTGGTGCTGGGACAGTTACTGAAGTAACT
GACTATACTACTGGCAGAGTTGGAGCACCTCTTATTTGCTGTGAAATTAAGCTAAAAGAC
TGGCAAGAAGGCGGTTATACAATTAATGACAAGCCAAACCCCAGAGGTGAAATCGTAATT
GGTGGACAGAACATCTCCATGGGATATTTTAAAAATGAAGAGAAAACAGCAGAAGATTAT
TCTGTGGATGAAAATGGACAAAGGTGGTTTTGCACTGGTGATATTGGAGAATTCCATCCC
GATGGATGTTTACAGATTATAGATCGTAAGAAAGATCTAGTGAAGTTACAAGCAGGAGAG
TATGTATCTCTTGGGAAAGTAGAAGCTGCACTGAAGAATTGTCCACTTATTGACAACATC
TGTGCTTTTGCCAAAAGTGATCAGTCCTATGTGATCAGTTTTGTGGTTCCTAACCAGAAA
AGGTTGACACTTTTGGCACAACAGAAAGGGGTAGAAGGAACTTGGGTTGATATCTGCAAT
AATCCTGCTATGGAAGCTGAAATACTGAAAGAAATTCGAGAAGCTGCAAATGCCATGAAA
TTGGAGCGATTTGAAATTCCAATCAAGGTTCGATTAAGCCCAGAGCCATGGACCCCTGAA
ACTGGTTTGGTAACTGATGCTTTCAAACTGAAAAGGAAGGAGCTGAGGAACCATTACCTC
AAAGACATTGAACGAATGTATGGGGGCAAATAA
Enzyme 35 GenBank Gene ID AF030555 Link Image
Enzyme 35 GeneCard ID ACSL4 Link Image
Enzyme 35 GenAtlas ID ACSL4 Link Image
Enzyme 35 HGNC ID HGNC:3571 Link Image
Enzyme 35 Chromosome Location X
Enzyme 35 Locus Xq22.3-q23
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Cao Y, Traer E, Zimmerman GA, McIntyre TM, Prescott SM: Cloning, expression, and chromosomal localization of human long-chain fatty acid-CoA ligase 4 (FACL4). Genomics. 1998 Apr 15;49(2):327-30. [PubMed Link Image]
  2. Piccini M, Vitelli F, Bruttini M, Pober BR, Jonsson JJ, Villanova M, Zollo M, Borsani G, Ballabio A, Renieri A: FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is deleted in a family with Alport syndrome, elliptocytosis, and mental retardation. Genomics. 1998 Feb 1;47(3):350-8. [PubMed Link Image]
  3. Meloni I, Muscettola M, Raynaud M, Longo I, Bruttini M, Moizard MP, Gomot M, Chelly J, des Portes V, Fryns JP, Ropers HH, Magi B, Bellan C, Volpi N, Yntema HG, Lewis SE, Schaffer JE, Renieri A: FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation. Nat Genet. 2002 Apr;30(4):436-40. Epub 2002 Mar 11. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 5849
Enzyme 36 Name Long-chain-fatty-acid--CoA ligase 1
Enzyme 36 Synonyms
  1. Long-chain acyl-CoA synthetase 1
  2. LACS 1
  3. Palmitoyl-CoA ligase 1
  4. Long-chain fatty acid CoA ligase 2
  5. Long-chain acyl-CoA synthetase 2
  6. LACS 2
  7. Acyl-CoA synthetase 1
  8. ACS1
  9. Palmitoyl-CoA ligase 2
Enzyme 36 Gene Name ACSL1
Enzyme 36 Protein Sequence >Long-chain-fatty-acid--CoA ligase 1
MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQ
SVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEW
LSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT
LGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQR
CGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAF
VKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQP
TVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKV
QSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV
GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGD
IGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAI
VVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHP
ELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV
Enzyme 36 Number of Residues 698
Enzyme 36 Molecular Weight 77944
Enzyme 36 Theoretical pI 7.16
Enzyme 36 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 36 General Function Lipid transport and metabolism
Enzyme 36 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate
Enzyme 36 Pathways
Enzyme 36 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • 25-45
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 219900 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID P33121 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name ACSL1_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >2097 bp
ATGCAAGCCCATGAGCTGTTCCGGTATTTTCGAATGCCAGAGCTGGTTGACTTCCGACAG
TACGTGCGTACTCTTCCGACCAACACGCTTATGGGCTTCGGAGCTTTTGCAGCACTCACC
ACCTTCTGGTACGCCACGAGACCCAAACCCCTGAAGCCGCCATGCGACCTCTCCATGCAG
TCAGTGGAAGTGGCGGGTAGTGGTGGTGCACGAAGATCCGCACTACTTGACAGCGACGAG
CCCTTGGTGTATTTCTATGATGATGTCACAACATTATACGAAGGTTTCCAGAGGGGAATA
CAGGTGTCAAATAATGGCCCTTGTTTAGGCTCTCGGAAACCAGACCAACCCTATGAATGG
CTTTCATATAAACAGGTTGCAGAATTGTCGGAGTGCATAGGCTCAGCACTGATCCAGAAG
GGCTTCAAGACTGCCCCAGATCAGTTCATTGGCATCTTTGCTCAAAATAGACCTGAGTGG
GTGATTATTGAACAAGGATGCTTTGCTTATTCGATGGTGATCGTTCCACTTTATGATACC
CTTGGAAATGAAGCCATCACGTACATAGTCAACAAAGCTGAACTCTCTCTGGTTTTTGTT
GACAAGCCAGAGAAGGCCAAACTCTTATTAGAGGGTGTAGAAAATAAGTTAATACCAGGC
CTTAAAATCATAGTTGTCATGGATGCCTACGGCAGTGAACTGGTGGAACGAGGCCAGAGG
TGTGGGGTGGAAGTCACCAGCATGAAGGCGATGGAGGACCTGGGAAGAGCCAACAGACGG
AAGCCCAAGCCTCCAGCACCTGAAGATCTTGCAGTAATTTGTTTCACAAGTGGAACTACA
GGCAACCCCAAAGGAGCAATGGTCACTCACCGAAACATAGTGAGCGATTGTTCAGCTTTT
GTGAAAGCAACAGAGAATACAGTCAATCCTTGCCCAGATGATACTTTGATATCTTTCTTG
CCTCTCGCCCATATGTTTGAGAGAGTTGTAGAGTGTGTAATGCTGTGTCATGGAGCTAAA
ATCGGATTTTTCCAAGGAGATATCAGGCTGCTCATGGATGACCTCAAGGTGCTTCAACCC
ACTGTCTTCCCCGTGGTTCCAAGACTGCTGAACCGGATGTTTGACCGAATTTTCGGACAA
GCAAACACCACGCTGAAGCGATGGCTCTTGGACTTTGCCTCCAAGAGGAAAGAAGCAGAG
CTTCGCAGCGGCATCATCAGAAACAACAGCCTGTGGGACCGGCTGATCTTCCACAAAGTA
CAGTCGAGCCTGGGCGGAAGAGTCCGGCTGATGGTGACAGGAGCCGCCCCGGTGTCTGCC
ACTGTGCTGACGTTCCTCAGAGCAGCCCTGGGCTGTCAGTTTTATGAAGGATACGGACAG
ACAGAGTGCACTGCCGGGTGCTGCCTAACCATGCCTGGAGACTGGACCGCAGGCCATGTT
GGGGCCCCGATGCCGTGCAATTTGATAAAACTTGTTGATGTGGAAGAAATGAATTACATG
GCTGCCGAGGGCGAGGGCGAGGTGTGTGTGAAAGGGCCAAATGTATTTCAGGGCTACTTG
AAGGACCCAGCGAAAACAGCAGAAGCTTTGGACAAAGACGGCTGGTTACACACAGGGGAC
ATTGGAAAATGGTTACCAAATGGCACCTTGAAAATTATCGACCGGAAAAAGCACATATTT
AAGCTGGCACAAGGAGAATACATAGCCCCTGAAAAGATTGAAAATATCTACATGCGAAGT
GAGCCTGTTGCTCAGGTGTTTGTCCACGGAGAAAGCCTGCAGGCATTTCTCATTGCAATT
GTGGTACCAGATGTTGAGACATTATGTTCCTGGGCCCAAAAGAGAGGATTTGAAGGGTCG
TTTGAGGAACTGTGCAGAAATAAGGATGTCAAAAAAGCTATCCTCGAAGATATGGTGAGA
CTTGGGAAGGATTCTGGTCTGAAACCATTTGAACAGGTCAAAGGCATCACATTGCACCCT
GAATTATTTTCTATCGACAATGGCCTTCTGACTCCAACAATGAAGGCGAAAAGGCCAGAG
CTGCGGAACTATTTCAGGTCGCAGATAGATGACCTCTATTCCACTATCAAGGTTTAG
Enzyme 36 GenBank Gene ID D10040 Link Image
Enzyme 36 GeneCard ID ACSL1 Link Image
Enzyme 36 GenAtlas ID ACSL1 Link Image
Enzyme 36 HGNC ID HGNC:3569 Link Image
Enzyme 36 Chromosome Location 4
Enzyme 36 Locus 4q34-q35
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Abe T, Fujino T, Fukuyama R, Minoshima S, Shimizu N, Toh H, Suzuki H, Yamamoto T: Human long-chain acyl-CoA synthetase: structure and chromosomal location. J Biochem (Tokyo). 1992 Jan;111(1):123-8. [PubMed Link Image]
  2. Ghosh B, Barbosa E, Singh I: Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression. Mol Cell Biochem. 1995 Oct 4;151(1):77-81. [PubMed Link Image]
  3. Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 5894
Enzyme 37 Name Long-chain-fatty-acid--CoA ligase 6
Enzyme 37 Synonyms
  1. Long-chain acyl-CoA synthetase 6
  2. LACS 6
Enzyme 37 Gene Name ACSL6
Enzyme 37 Protein Sequence >Long-chain-fatty-acid--CoA ligase 6
MQTQEILRILRLPELGDLGQFFRSLSATTLVSMGALAAILAYWFTHRPKALQPPCNLLMQ
SEEVEDSGGARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPKQPYQW
LSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDT
LGPGAIRYIINTADISTVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKERGQK
CGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF
LKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCP
TIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKI
QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV
GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGD
IGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGI
VVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHS
DMFSVQNGLLTPTLKAKRPELREYFKKQIEELYSISM
Enzyme 37 Number of Residues 697
Enzyme 37 Molecular Weight 77753
Enzyme 37 Theoretical pI 7.46
Enzyme 37 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 37 General Function Lipid transport and metabolism
Enzyme 37 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid
Enzyme 37 Pathways
Enzyme 37 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • 1-37
Enzyme 37 Transmembrane Regions Not Available
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 5702202 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q9UKU0 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name ACSL6_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >2094 bp
ATGCAGACACAGGAGATCCTGAGGATACTGCGACTGCCTGAGCTAGGTGACTTGGAACAG
TTTTTCCGCAGCCTCTCGGCCACCACCCTCGTGAGTATGGGTGCCCTGGCTGCCATCCTT
GCCTACTGGTTCACTCAGCGGCCAAAGGCCTTGCAGCCGCCATGCAACCTCCTGATGCAG
TCAGAAGAAGTAGAGGACAGTGGCGGGGCACGGCGATCTGTGATTGGGTCTGGCCCTCAG
CTACTTACCCACTACTATGATGATGCCCGGACCATGTACCAGGTGTTCCGCCGTGGGCTT
AGCATCTCAGGGAATGGGCCCTGTCTTGGTTTCAGGAAGCCTAAGCAGCCTTACCAGTGG
CTGTCCTACCAGGAGGTGGCCGACAGGGCTGAATTTCTGGGGTCCGGACTTCTCCAGCAC
AATTGTAAAGCATGCACTGATCAGTTTATTGGTGTTTTTGCACAAAATCGGCCAGAGTGG
ATCATTGTGGAGCTGGCCTGCTACACATATTCCATGGTGGTGGTCCCGCTCTATGACACC
CTGGGCCCTGGGGCTATCCGCTACATCATCAATACAGCGGACATCAGCACCGTGATTGTG
GACAAACCTCAGAAGGCTGTGCTTCTGCTAGAGCATGTGGAGAGGAAGGAGACTCCAGGC
CTCAAGCTGATCATCCTCATGGACCCATTCGAAGAAGCCCTGAAAGAGAGAGGGCAGAAG
TGCGGGGTGGTCATTAAGTCCATGCAGGCCGTGGAGGACTGTGGCCAAGAGAATCACCAG
GCTCCTGTGCCCCCGCAGCCTGATGACCTCTCCATTGTGTGTTTCACAAGCGGCACGACA
GGGAACCCAAAAGGTGCGATGCTCACCCATGGGAACGTGGTGGCTGATTTCTCAGGCTTT
CTGAAAGTGACAGAGAGTCAGTGGGCTCCCACTTGTGCGGATGTGCACATTTCCTATTTG
CCTTTAGCACACATGTTTGAGCGAATGGTGCAGTCTGTCGTCTATTGCCACGGAGGGCGT
GTTGGCTTCTTCCAGGGAGATATCCGCCTTCTCTCAGATGACATGAAGGCTCTATGCCCC
ACCATCTTCCCTGTGGTCCCACGACTGCTGAACCGGATGTACGACAAGATCTTCAGCCAG
GCAAACACACCATTAAAGCGCTGGCTCCTGGAGTTTGCAGCAAAGCGTAAGCAAGCCGAG
GTCCGGAGTGGAATCATCAGGAATGATAGTATCTGGGATGAACTCTTCTTTAATAAGATT
CAGGCCAGTCTTGGTGGGTGTGTGCGGATGATTGTTACTGGAGCAGCCCCAGCATCACCA
ACAGTTCTGGGATTTCTCCGGGCAGCTCTAGGGTGCCAGGTTTATGAAGGTTATGGCCAA
ACTGAGTGCACAGCTGGATGTACCTTCACCACTCCTGGCGACTGGACCTCAGGGCACGTA
GGGGCGCCACTTCCCTGCAATCATATCAAGCTCGTTGATGTTGAGGAACTGAACTACTGG
GCCTGCAAAGGAGAGGGAGAGATATGTGTGAGAGGACCAAATGTGTTCAAAGGCTACTTG
AAAGATCCAGACAGGACGAAGGAGGCCCTGGACAGCGATGGCTGGCTTCACACTGGAGAC
ATCGGAAAATGGCTGCCGGCAGGAACTCTTAAAATTATTGATCGGAAAAAGCATATATTT
AAACTTGCTCAGGGAGAATATGTTGCACCCGAGAAGATTGAGAACATCTACATCCGGAGC
CAACCTGTGGCGCAAATCTATGTCCATGGGGACAGCTTAAAGGCCTTTTTGGTAGGCATT
GTTGTGCCTGACCCTGAAGTTATGCCCTCCTGGGCCCAGAAGAGAGGAATTGAAGGAACA
TATGCAGATCTCTGCACAAATAAGGATCTGAAGAAAGCCATTTTGGAAGATATGGTGAGG
TTAGGAAAAGAAAGTGGACTCCATTCTTTTGAGCAGGTTAAAGCCATTCACATCCATTCT
GACATGTTCTCAGTTCAAAATGGCTTGCTGACCCCAACACTAAAAGCTAAGAGACCTGAG
CTGAGAGAGTACTTCAAAAAACAAATAGAAGAGCTTTACTCAATCCCCATGTGA
Enzyme 37 GenBank Gene ID AF129166 Link Image
Enzyme 37 GeneCard ID ACSL6 Link Image
Enzyme 37 GenAtlas ID ACSL6 Link Image
Enzyme 37 HGNC ID HGNC:16496 Link Image
Enzyme 37 Chromosome Location Not Available
Enzyme 37 Locus Not Available
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed Link Image]
  2. Yagasaki F, Jinnai I, Yoshida S, Yokoyama Y, Matsuda A, Kusumoto S, Kobayashi H, Terasaki H, Ohyashiki K, Asou N, Murohashi I, Bessho M, Hirashima K: Fusion of TEL/ETV6 to a novel ACS2 in myelodysplastic syndrome and acute myelogenous leukemia with t(5;12)(q31;p13). Genes Chromosomes Cancer. 1999 Nov;26(3):192-202. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 5916
Enzyme 38 Name Long-chain-fatty-acid--CoA ligase 5
Enzyme 38 Synonyms
  1. Long-chain acyl-CoA synthetase 5
  2. LACS 5
Enzyme 38 Gene Name ACSL5
Enzyme 38 Protein Sequence >Long-chain-fatty-acid--CoA ligase 5
MLFIFNFLFSPLPTPALICILTFGAAIFLWLITRPQPVLPLLDLNNQSVGIEGGARKGVS
QKNNDLTSCCFSDAKTMYEVFQRGLAVSDNGPCLGYRKPNQPYRWLSYKQVSDRAEYLGS
CLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVHIVNKADI
AMVICDTPQKALVLIGNVEKGFTPSLKVIILMDPFDDDLKQRGEKSGIEILSLYDAENLG
KEHFRKPVPPSPEDLSVICFTSGTTGDPKGAMITHQNIVSNAAAFLKCVEHAYEPTPDDV
AISYLPLAHMFERIVQAVVYSCGARVGFFQGDIRLLADDMKTLKPTLFPAVPRLLNRIYD
KVQNEAKTPLKKFLLKLAVSSKFKELQKGIIRHDSFWDKLIFAKIQDSLGGRVRVIVTGA
APMSTSVMTFFRAAMGCQVYEAYGQTECTGGCTFTLPGDWTSGHVGVPLACNYVKLEDVA
DMNYFTVNNEGEVCIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDR
KKNIFKLAQGEYIAPEKIENIYNRSQPVLQIFVHGESLRSSLVGVVVPDTDVLPSFAAKL
GVKGSFEELCQNQVVREAILEDLQKIGKESGLKTFEQVKAIFLHPEPFSIENGLLTPTLK
AKRGELSKYFRTQIDSLYEHIQD
Enzyme 38 Number of Residues 683
Enzyme 38 Molecular Weight 75992
Enzyme 38 Theoretical pI 6.91
Enzyme 38 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 38 General Function Lipid transport and metabolism
Enzyme 38 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids
Enzyme 38 Pathways
Enzyme 38 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • 1-35
Enzyme 38 Transmembrane Regions Not Available
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 6174680 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID Q9ULC5 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name ACSL5_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >2052 bp
ATGCTTTTTATCTTTAACTTTTTGTTTTCCCCACTTCCGACCCCGGCGTTGATCTGCATC
CTGACATTTGGAGCTGCCATCTTCTTGTGGCTGATCACCAGACCTCAACCCGTCTTACCT
CTTCTTGACCTGAACAATCAGTCTGTGGGAATTGAGGGAGGAGCACGGAAGGGGGTTTCC
CAGAAGAACAATGACCTAACAAGTTGCTGCTTCTCAGATGCCAAGACTATGTATGAGGTT
TTCCAAAGAGGACTCGCTGTGTCTGACAATGGGCCCTGCTTGGGATATAGAAAACCAAAC
CAGCCCTACAGATGGCTATCTTACAAACAGGTGTCTGATAGAGCAGAGTACCTGGGTTCC
TGTCTCTTGCATAAAGGTTATAAATCATCACCAGACCAGTTTGTCGGCATCTTTGCTCAG
AATAGGCCAGAGTGGATCATCTCCGAATTGGCTTGTTACACGTACTCTATGGTAGCTGTA
CCTCTGTATGACACCTTGGGACCAGAAGCCATCGTACATATTGTCAACAAGGCTGATATC
GCCATGGTGATCTGTGACACACCCCAAAAGGCATTGGTGCTGATAGGGAATGTAGAGAAA
GGCTTCACCCCGAGCCTGAAGGTGATCATCCTTATGGACCCCTTTGATGATGACCTGAAG
CAAAGAGGGGAGAAGAGTGGAATTGAGATCTTATCCCTATATGATGCTGAGAACCTAGGC
AAAGAGCACTTCAGAAAACCTGTGCCTCCTAGCCCAGAAGACCTGAGCGTCATCTGCTTC
ACCAGTGGGACCACAGGTGACCCCAAAGGAGCCATGATAACCCATCAAAATATTGTTTCA
AATGCTGCTGCCTTTCTCAAATGTGTGGAGCATGCTTATGAGCCCACTCCTGATGATGTG
GCCATATCCTACCTCCCTCTGGCTCATATGTTTGAGAGGATTGTACAGGCTGTTGTGTAC
AGCTGTGGAGCCAGAGTTGGATTCTTCCAAGGGGATATTCGGTTGCTGGCTGACGACATG
AAGACTTTGAAGCCCACATTGTTTCCCGCGGTGCCTCGACTCCTTAACAGGATCTACGAT
AAGGTACAAAATGAGGCCAAGACACCCTTGAAGAAGTTCTTGTTGAAGCTGGCTGTTTCC
AGTAAATTCAAAGAGCTTCAAAAGGGTATCATCAGGCATGATAGTTTCTGGGACAAGCTC
ATCTTTGCAAAGATCCAGGACAGCCTGGGCGGAAGGGTTCGTGTAATTGTCACTGGAGCT
GCCCCCATGTCCACTTCAGTCATGACATTCTTCCGGGCAGCAATGGGATGTCAGGTGTAT
GAAGCTTATGGTCAAACAGAATGCACAGGTGGCTGTACATTTACATTACCTGGGGACTGG
ACATCAGGTCACGTTGGGGTGCCCCTGGCTTGCAATTACGTGAAGCTGGAAGATGTGGCT
GACATGAACTACTTTACAGTGAATAATGAAGGAGAGGTCTGCATCAAGGGTACAAACGTG
TTCAAAGGATACCTGAAGGACCCTGAGAAGACACAGGAAGCCCTGGACAGTGATGGCTGG
CTTCACACAGGAGACATTGGTCGCTGGCTCCCGAATGGAACTCTGAAGATCATCGACCGT
AAAAAGAACATTTTCAAGCTGGCCCAAGGAGAATACATTGCACCAGAGAAGATAGAAAAT
ATCTACAACAGGAGTCAACCAGTGTTACAAATTTTTGTACACGGGGAGAGCTTACGGTCA
TCCTTAGTAGGAGTGGTGGTTCCTGACACAGATGTACTTCCCTCATTTGCAGCCAAGCTT
GGGGTGAAGGGCTCCTTTGAGGAACTGTGCCAAAACCAAGTTGTAAGGGAAGCCATTTTA
GAAGACTTGCAGAAAATTGGGAAAGAAAGTGGCCTTAAAACTTTTGAACAGGTCAAAGCC
ATTTTTCTTCATCCAGAGCCATTTTCCATTGAAAATGGGCTCTTGACACCAACATTGAAA
GCAAAGCGAGGAGAGCTTTCCAAATACTTTCGGACCCAAATTGACAGCCTGTATGAGCAC
ATCCAGGATTAG
Enzyme 38 GenBank Gene ID AB033899 Link Image
Enzyme 38 GeneCard ID ACSL5 Link Image
Enzyme 38 GenAtlas ID ACSL5 Link Image
Enzyme 38 HGNC ID HGNC:16526 Link Image
Enzyme 38 Chromosome Location 10
Enzyme 38 Locus 10q25.1-q25.2
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 5919
Enzyme 39 Name Long-chain-fatty-acid--CoA ligase 3
Enzyme 39 Synonyms
  1. Long-chain acyl-CoA synthetase 3
  2. LACS 3
Enzyme 39 Gene Name ACSL3
Enzyme 39 Protein Sequence >Long-chain-fatty-acid--CoA ligase 3
MNNHVSSKPSTMKLKHTINPILLYFIHFLISLYTILTYIPFYFFSESRQEKSNRIKAKPV
NSKPDSAYRSVNSLDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEDEVQPN
GKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACF
MYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGK
PPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMIS
HSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQ
SSKIKKGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQI
SKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTES
AGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYY
KNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAA
LKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLK
VLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK
Enzyme 39 Number of Residues 720
Enzyme 39 Molecular Weight 80421
Enzyme 39 Theoretical pI 8.51
Enzyme 39 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 39 General Function Lipid transport and metabolism
Enzyme 39 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates
Enzyme 39 Pathways
Enzyme 39 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • 1-31
Enzyme 39 Transmembrane Regions Not Available
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 4165018 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID O95573 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name ACSL3_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >2163 bp
ATGAATAACCACGTGTCTTCAAAACCATCTACCATGAAGCTAAAACATACCATCAACCCT
ATTCTTTTATATTTTATACATTTTCTAATATCACTTTATACTATTTTAACATACATTCCG
TTTTATTTTTTCTCCGAGTCAAGACAAGAAAAATCAAACCGAATTAAAGCAAAGCCTGTA
AATTCAAAACCTGATTCTGCATACAGATCTGTTAATAGTTTGGATGGTTTGGCTTCAGTA
TTATACCCTGGATGTGATACTTTAGATAAAGTTTTTACATATGCAAAAAACAAATTTAAG
AACAAAAGACTCTTGGGAACACGTGAAGTTTTAAATGAGGAAGATGAAGTACAACCAAAT
GGAAAAATTTTTAAAAAGGTTATTCTTGGACAGTATAATTGGCTTTCCTATGAAGATGTC
TTTGTTCGAGCCTTTAATTTTGGAAATGGATTACAGATGTTGGGTCAGAAACCAAAGACC
AACATCGCCATCTTCTGTGAGACCAGGGCCGAGTGGATGATAGCTGCACAGGCGTGTTTT
ATGTATAATTTTCAGCTTGTTACATTATATGCCACTCTAGGAGGTCCAGCCATTGTTCAT
GCATTAAATGAAACAGAGGTGACCAACATCATTACTAGTAAAGAACTCTTACAAACAAAG
TTGAAGGATATAGTTTCTTTGGTCCCACGCCTGCGGCACATCATCACTGTTGATGGAAAG
CCACCGACCTGGTCCGACTTCCCCAAGGGCATCATTGTGCATACCATGGCTGCAGTGGAG
GCCCTGGGAGCCAAGGCCAGCATGGAAAACCAACCTCATAGCAAACCATTGCCCTCAGAT
ATTGCAGTAATCATGTACACAAGTGGATCCACAGGACTTCCAAAGGGAGTCATGATCTCA
CATAGTAACATTATTGCTGGTATAACTGGGATGGCAGAAAGGATTCCAGAACTAGGAGAG
GAAGATGTCTACATTGGATATTTGCCTCTGGCCCATGTTCTAGAATTAAGTGCTGAGCTT
GTCTGTCTTTCTCACGGATGCCGCATTGGTTACTCTTCACCACAGACTTTAGCAGATCAG
TCTTCAAAAATTAAAAAAGGAAGCAAAGGGGATACATCCATGTTGAAACCAACACTGATG
GCAGCAGTTCCGGAAATCATGGATCGGATCTACAAAAATGTCATGAATAAAGTCAGTGAA
ATGAGTAGTTTTCAACGTAATCTGTTTATTCTGGCCTATAATTACAAAATGGAACAGATT
TCAAAAGGACGTAATACTCCACTGTGCGACAGCTTTGTTTTCCGGAAAGTTCGAAGCTTG
CTAGGGGGAAATATTCGTCTCCTGTTGTGTGGTGGCGCTCCACTTTCTGCAACCACGCAG
CGATTCATGAACATCTGTTTCTGCTGTCCTGTTGGTCAGGGATACGGGCTCACTGAATCT
GCTGGGGCTGGAACAATTTCCGAAGTGTGGGACTACAATACTGGCAGAGTGGGAGCACCA
TTAGTTTGCTGTGAAATCAAATTAAAAAACTGGGAGGAAGGTGGATACTTTAATACTGAT
AAGCCACACCCCAGGGGTGAAATTCTTATTGGGGGCCAAAGTGTGACAATGGGGTACTAC
AAAAATGAAGCAAAAACAAAAGCTGATTTCTCTGAAGATGAAAATGGACAAAGGTGGCTC
TGTACTGGGGATATTGGAGAGTTTGAACCCGATGGATGCTTAAAGATTATTGATCGTAAA
AAGGACCTTGTAAAACTACAGGCAGGGGAATATGTTTCTCTTGGGAAAGTAGAGGCAGCT
TTGAAGAATCTTCCACTAGTAGATAACATTTGTGCATATGCAAACAGTTATCATTCTTAT
GTCATTGGATTTGTTGTGCCAAATCAAAAGGAACTAACTGAACTAGCTCGAAAGAAAGGA
CTTAAAGGGACTTGGGAGGAGCTGTGTAACAGTTGTGAAATGGAAAATGAGGTACTTAAA
GTGCTTTCCGAAGCTGCTATTTCAGCAAGTCTGGAAAAGTTTGAAATTCCAGTAAAAATT
CGTTTGAGTCCTGAACCGTGGACCCCTGAAACTGGTCTGGTGACAGATGCCTTCAAGCTG
AAACGCAAAGAGCTTAAAACACATTACCAGGCGGACATTGAGCGAATGTATGGAAGAAAA
TAA
Enzyme 39 GenBank Gene ID D89053 Link Image
Enzyme 39 GeneCard ID ACSL3 Link Image
Enzyme 39 GenAtlas ID ACSL3 Link Image
Enzyme 39 HGNC ID HGNC:3570 Link Image
Enzyme 39 Chromosome Location 2
Enzyme 39 Locus 2q34-q35
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Minekura H, Fujino T, Kang MJ, Fujita T, Endo Y, Yamamoto TT: Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35. Genomics. 1997 May 15;42(1):180-1. [PubMed Link Image]
  2. Minekura H, Kang MJ, Inagaki Y, Suzuki H, Sato H, Fujino T, Yamamoto TT: Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene. Gene. 2001 Oct 31;278(1-2):185-92. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 6335
Enzyme 40 Name Cytosolic acyl coenzyme A thioester hydrolase
Enzyme 40 Synonyms
  1. Long chain acyl-CoA thioester hydrolase
  2. CTE-II
  3. CTE-IIa
  4. Brain acyl-CoA hydrolase
  5. Acyl-CoA thioesterase 7
Enzyme 40 Gene Name ACOT7
Enzyme 40 Protein Sequence >Cytosolic acyl coenzyme A thioester hydrolase
MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIM
RPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGE
VAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVV
YSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCT
LHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTS
NKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEE
GKGRYLQMKAKRQGHAEPQP
Enzyme 40 Number of Residues 380
Enzyme 40 Molecular Weight 41797
Enzyme 40 Theoretical pI 8.66
Enzyme 40 GO Classification
Function
  • catalytic activity
Process
Component
Enzyme 40 General Function Lipid transport and metabolism
Enzyme 40 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl- CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • 1-19
Enzyme 40 Transmembrane Regions Not Available
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 2780414 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID O00154 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name BACH_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1017 bp
ATGTCGGGCCCAGACGTCGAGACGCCGTCCGCCATCCAGATCTGCCGGATCATGCGGCCA
GATGATGCCAACGTGGCCGGCAATGTCCACGGGGGGACCATCCTGAAGATGATCGAGGAG
GCAGGCGCCATCATCAGCACCCGGCATTGCAACAGCCAGAACGGGGAGCGCTGTGTGGCC
GCCCTGGCTCGTGTCGAGCGCACCGACTTCCTGTCTCCCATGTGCATCGGTGAGGTGGCG
CATGTCAGCGCGGAGATCACCTACACCTCCAAGCACTCTGTGGAGGTGCAGGTCAACGTG
ATGTCCGAAAACATCCTCACAGGTGCCAAAAAGCTGACCAATAAGGCCACCCTGTGGTAT
GTGCCCCTGTCGCTGAAGAATGTGGACAAGGTCCTCGAGGTGCCTCCTGTTGTGTATTCC
CGGCAGGAGCAGGAGGAGGAGGGCCGGAAGCGGTATGAAGCCCAGAAGCTGGAGCGCATG
GAGACCAAGTGGAGGAACGGGGACATCGTCCAGCCAGTCCTCAACCCAGAGCCGAACACT
GTCAGCTACAGCCAGTCCAGCTTGATCCACCTGGTGGGGCCTTCAGACTGCACCCTGCAC
GGCTTTGTGCACGGAGGTGTGACCATGAAGCTCATGGATGAGGTCGCCGGGATCGTGGCT
GCACGCCACTGCAAGACCAACATCGTCACAGCTTCCGTGGACGCCATTAATTTTCATGAC
AAGATCAGAAAAGGCTGCGTCATCACCATCTCGGGACGCATGACCTTCACGAGCAATAAG
TCCATGGAGATCGAGGTGTTGGTGGACGCCGACCCTGTTGTGGACAGCTCTCAGAAGCGC
TACCGGGCCGCCAGTGCCTTCTTCACCTACGTGTCGCTGAGCCAGGAAGGCAGGTCGCTG
CCTGTGCCCCAGCTGGTGCCCGAGACCGAGGACGAGAAGAAGCGCTTTGAGGAAGGCAAA
GGGCGGTACCTGCAGATGAAGGCGAAGCGACAGGGCCACGCGGAGCCTCAGCCCTAG
Enzyme 40 GenBank Gene ID D88894 Link Image
Enzyme 40 GeneCard ID ACOT7 Link Image
Enzyme 40 GenAtlas ID ACOT7 Link Image
Enzyme 40 HGNC ID HGNC:24157 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 1p36.31-p36.11
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Yamada J, Kurata A, Hirata M, Taniguchi T, Takama H, Furihata T, Shiratori K, Iida N, Takagi-Sakuma M, Watanabe T, Kurosaki K, Endo T, Suga T: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase. J Biochem (Tokyo). 1999 Dec;126(6):1013-9. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 6336
Enzyme 41 Name Acyl-coenzyme A thioesterase 2
Enzyme 41 Synonyms
  1. Acyl-CoA thioesterase 2
  2. Peroxisomal acyl-coenzyme A thioester hydrolase 2a
  3. Peroxisomal long-chain acyl-coA thioesterase 2
  4. ZAP128
  5. CTE-Ia
Enzyme 41 Gene Name ACOT2
Enzyme 41 Protein Sequence >Acyl-coenzyme A thioesterase 2
MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVP
ARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLG
ELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGR
LLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLL
AGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELC
LSMASFLKGITAAVVINGSVANVGGTLRYKGETLPPVGVNRNRIKVTKDGYADIVDVLNS
PLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPET
GHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGREGTIP
SKV
Enzyme 41 Number of Residues 483
Enzyme 41 Molecular Weight 53257
Enzyme 41 Theoretical pI 8.93
Enzyme 41 GO Classification
Function
  • CoA hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 41 General Function Not Available
Enzyme 41 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 887376 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID P49753 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name ACOT2_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >937 bp
CCCCCGGGCTGCAGGAATTCCTGAATTCAAAATGGCCTCATCTCCTGCTGTCCTTCGAGC
GTCCCGGCTGTACCAATGGAGCCTGAAGAGTTCGGCGCAGTTCCTGGGGTCTCCACAGCT
GAGGCAGAACCTGGGCCCTTTCCTGGGATTGTGGACATGTTCGGGAACTGGAGGTGGCCT
GCTGGAGTATCGGGCTAGTCTGCTGGCTGGGAAGGGTTTTGCTGTGATGGCTCTGGCTTA
TTATAACTATGAAGACCTCCCCAAGACCATGGAGACGCTCCATCTGGAGTACTTTGAAGA
AGCCATGAACTACTTGCTCAGTCATCCCGAGGTAAAAGGTCCAGGAGTTGGGCTGCTTGG
AATTTCCAAAGGGGGTGAGCTCTGCCTTTCCATGGCCTCTTTCCTGAAGGGCATCACGGC
TGCTGTCGTCATCAACGGCTCTGTGGCCAATGTTGGGGGAACCTTACACTACAAGGGCGA
GACCCTGCCCCCTGTGGGCGTCAACAGAAATCGCATCAAGGTGACCAAAGATGGCTATGC
AGACATTGTGGATGTCCTGAACAGCCCTTTGGAAGGACCTGACCAGAAGAGCTTCATTCC
TGTGGAAAGGGCAGAGAGCACCTTCCTGTTCCTGGTAGGTCAGGATGACCACAACTGGAA
GAGTGAGTTCTATGCTAATGAGGCCTGTAAACGCTTGCAGGCCCATGGGAGGAGAAAGCC
CCAGATCATCTGTTACCCAGAGACAGGGCACTATATTGAGCCTCCTTACTTCCCCCTGTG
TCGGGCTTCCCTGCATGCCTTGGTGGGCAGTCCTATTATCTGGGGAGGGGAGCCCAGGGC
TCATGCCATGGCTCAGGTGGATGCTTGGAAACAACTCCAGACTTTCTTCCACAAACACTT
GGGTGGCCACGAGGGGACAATCCCATCAAAAGTGTAA
Enzyme 41 GenBank Gene ID L40401 Link Image
Enzyme 41 GeneCard ID ACOT2 Link Image
Enzyme 41 GenAtlas ID ACOT2 Link Image
Enzyme 41 HGNC ID HGNC:18431 Link Image
Enzyme 41 Chromosome Location 14
Enzyme 41 Locus 14q24.3
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, Holman K, et al.: Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature. 1995 Jun 29;375(6534):754-60. [PubMed Link Image]
  2. Jones JM, Gould SJ: Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. Biochem Biophys Res Commun. 2000 Aug 18;275(1):233-40. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 6338
Enzyme 42 Name Acyl-coenzyme A thioesterase 8
Enzyme 42 Synonyms
  1. Choloyl-coenzyme A thioesterase
  2. Acyl-CoA thioesterase 8
  3. Peroxisomal acyl-coenzyme A thioester hydrolase 1
  4. PTE-1
  5. Peroxisomal long-chain acyl-coA thioesterase 1
  6. HIV-Nef-associated acyl coA thioesterase
  7. Thioesterase II
  8. hTE
  9. hACTEIII
  10. hACTE-III
  11. PTE-2
Enzyme 42 Gene Name ACOT8
Enzyme 42 Protein Sequence >Acyl-coenzyme A thioesterase 8
MSSPQAPEDGQGCGDRGDPPGDLRSVLVTTVLNLEPLDEDLFRGRHYWVPAKRLFGGQIV
GQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSVKAVQHGKP
IFICQASFQQAQPSPMQHQFSMPTVPPPEELLDCETLIDQYLRDPNLQKRYPLALNRIAA
QEVPIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEGDMKMHCCVAAYISDYAFLGTAL
LPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAV
TCAQEGVIRVKPQVSESKL
Enzyme 42 Number of Residues 319
Enzyme 42 Molecular Weight 35915
Enzyme 42 Theoretical pI 7.60
Enzyme 42 GO Classification
Function
  • CoA hydrolase activity
  • acyl-CoA thioesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • thiolester hydrolase activity
Process
  • acyl-CoA metabolism
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
Enzyme 42 General Function Lipid transport and metabolism
Enzyme 42 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA:amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs. May be involved in the metabolic regulation of peroxisome proliferation
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 2318125 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID O14734 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name ACOT8_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >960 bp
ATGTCGTCCCCGCAGGCCCCAGAAGATGGGCAGGGCTGTGGCGACCGCGGCGATCCCCCT
GGGGACCTCCGTAGCGTCTTGGTCACGACCGTGCTCAACCTCGAGCCGCTGGACGAGGAT
CTCTTCAGAGGAAGGCATTACTGGGTACCGGCCAAGAGGCTGTTTGGTGGTCAGATCGTG
GGCCAGGCCCTGGTGGCTGCAGCCAAGTCTGTGAGTGAAGACGTCCACGTGCACTCCCTG
CACTGCTACTTTGTTCGGGCAGGGGACCCGAAGCTGCCAGTACTGTACCAAGTGGAGCGG
ACACGAACAGGGTCGAGCTTCTCGGTGCGCTCTGTGAAGGCCGTGCAACATGGGAAGCCC
ATCTTCATCTGCCAGGCCTCCTTCCAGCAGGCCCAGCCCAGCCCCATGCAGCACCAGTTC
TCCATGCCCACTGTGCCACCACCAGAAGAGCTGCTTGACTGTGAGACCCTCATTGACCAG
TATTTAAGGGACCCTAACCTCCAAAAGAGGTACCCATTGGCGCTCAACCGAATTGCTGCT
CAGGAGGTCCCCATTGAGATCAAGCCAGTAAACCCATCCCCCCTGAGCCAGCTGCAGAGA
ATGGAGCCCAAACAGATGTTCTGGGTGCGAGCCCGGGGCTATATTGGCGAGGGCGACATG
AAGATGCACTGCTGCGTGGCCGCCTATATCTCCGACTATGCCTTCTTGGGCACTGCACTG
CTGCCTCACCAGTGGCAGCACAAGGTGCACTTCATGGTCTCACTGGACCATTCCATGTGG
TTCCACGCCCCCTTCCGAGCTGACCACTGGATGCTCTATGAATGCGAGAGCCCCTGGGCC
GGTGGCTCTCGGGGGCTGGTCCATGGGCGGCTGTGGCGTCAGGATGGAGTCCTAGCTGTG
ACCTGTGCCCAGGAGGGCGTGATCCGAGTGAAGCCCCAGGTCTCAGAGAGCAAGCTGTAG
Enzyme 42 GenBank Gene ID AF014404 Link Image
Enzyme 42 GeneCard ID ACOT8 Link Image
Enzyme 42 GenAtlas ID ACOT8 Link Image
Enzyme 42 HGNC ID HGNC:15919 Link Image
Enzyme 42 Chromosome Location 20
Enzyme 42 Locus 20q13.12
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Watanabe H, Shiratori T, Shoji H, Miyatake S, Okazaki Y, Ikuta K, Sato T, Saito T: A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. Biochem Biophys Res Commun. 1997 Sep 8;238(1):234-9. [PubMed Link Image]
  2. Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S: Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. J Biol Chem. 1997 May 23;272(21):13779-85. [PubMed Link Image]
  3. Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ: Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. J Biol Chem. 1999 Apr 2;274(14):9216-23. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Hunt MC, Alexson SE: The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog Lipid Res. 2002 Mar;41(2):99-130. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 6339
Enzyme 43 Name Palmitoyl-protein thioesterase 1 precursor
Enzyme 43 Synonyms
  1. PPT-1
  2. Palmitoyl-protein hydrolase 1
Enzyme 43 Gene Name PPT1
Enzyme 43 Protein Sequence >Palmitoyl-protein thioesterase 1 precursor
MASPGCLWLLAVALLPWTCASRALQHLDPPAPLPLVIWHGMGDSCCNPLSMGAIKKMVEK
KIPGIYVLSLEIGKTLMEDVENSFFLNVNSQVTTVCQALAKDPKLQQGYNAMGFSQGGQF
LRAVAQRCPSPPMINLISVGGQHQGVFGLPRCPGESSHICDFIRKTLNAGAYSKVVQERL
VQAEYWHDPIKEDVYRNHSIFLADINQERGINESYKKNLMALKKFVMVKFLNDSIVDPVD
SEWFGFYRSGQAKETIPLQETSLYTQDRLGLKEMDNAGQLVFLATEGDHLQLSEEWFYAH
IIPFLG
Enzyme 43 Number of Residues 306
Enzyme 43 Molecular Weight 34194
Enzyme 43 Theoretical pI 6.50
Enzyme 43 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-(protein) hydrolase activity
  • thiolester hydrolase activity
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein modification
Component
Enzyme 43 General Function Not Available
Enzyme 43 Specific Function Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions
  • palmitoyl[protein] + H2O = palmitate + protein
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • 1-27
Enzyme 43 Transmembrane Regions Not Available
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 1160967 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID P50897 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name PPT1_HUMAN Link Image
Enzyme 43 PDB ID 1EXW Link Image
Enzyme 43 PDB File Show
Enzyme 43 3D Structure
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >921 bp
ATGGCGTCGCCCGGCTGCCTGTGGCTCTTGGCTGTGGCTCTCCTGCCATGGACCTGCGCT
TCTCGGGCGCTGCAGCATCTGGACCCGCCGGCGCCGCTGCCGTTGGTGATCTGGCATGGG
ATGGGAGACAGCTGTTGCAATCCCTTAAGCATGGGTGCTATTAAAAAAATGGTGGAGAAG
AAAATACCTGGAATTTACGTCTTATCTTTAGAGATTGGGAAGACCCTGATGGAGGACGTG
GAGAACAGCTTCTTCTTGAATGTCAATTCCCAAGTAACAACAGTGTGTCAGGCACTTGCT
AAGGATCCTAAATTGCAGCAAGGCTACAATGCTATGGGATTCTCCCAGGGAGGCCAATTT
CTGAGGGCAGTGGCTCAGAGATGCCCTTCACCTCCCATGATCAATCTGATCTCGGTTGGG
GGACAACATCAAGGTGTTTTTGGACTCCCTCGATGCCCAGGAGAGAGCTCTCACATCTGT
GACTTCATCCGAAAAACACTGAATGCTGGGGCGTACTCCAAAGTTGTTCAGGAACGCCTC
GTGCAAGCCGAATACTGGCATGACCCCATAAAGGAGGATGTGTATCGCAACCACAGCATC
TTCTTGGCAGATATAAATCAGGAGCGGGGTATCAATGAGTCCTACAAGAAAAACCTGATG
GCCCTGAAGAAGTTTGTGATGGTGAAATTCCTCAATGATTCCATTGTGGACCCTGTAGAT
TCGGAGTGGTTTGGATTTTACAGAAGTGGCCAAGCCAAGGAAACCATTCCCTTACAGGAG
ACCTCCCTGTACACACAGGACCGCCTGGGGCTAAAGGAAATGGACAATGCAGGACAGCTA
GTGTTTCTGGCTACAGAAGGGGACCATCTTCAGTTGTCTGAAGAATGGTTTTATGCCCAC
ATCATACCATTCCTTGGATGA
Enzyme 43 GenBank Gene ID L42809 Link Image
Enzyme 43 GeneCard ID PPT1 Link Image
Enzyme 43 GenAtlas ID PPT1 Link Image
Enzyme 43 HGNC ID HGNC:9325 Link Image
Enzyme 43 Chromosome Location 1
Enzyme 43 Locus 1p32
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Vesa J, Hellsten E, Verkruyse LA, Camp LA, Rapola J, Santavuori P, Hofmann SL, Peltonen L: Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis. Nature. 1995 Aug 17;376(6541):584-7. [PubMed Link Image]
  2. Crews CM, Lane WS, Schreiber SL: Didemnin binds to the protein palmitoyl thioesterase responsible for infantile neuronal ceroid lipofuscinosis. Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4316-9. [PubMed Link Image]
  3. Schriner JE, Yi W, Hofmann SL: cDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT), the enzyme defective in infantile neuronal ceroid lipofuscinosis. Genomics. 1996 Jun 15;34(3):317-22. [PubMed Link Image]
  4. Lu JY, Verkruyse LA, Hofmann SL: Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase. Proc Natl Acad Sci U S A. 1996 Sep 17;93(19):10046-50. [PubMed Link Image]
  5. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
  6. Mitchison HM, Hofmann SL, Becerra CH, Munroe PB, Lake BD, Crow YJ, Stephenson JB, Williams RE, Hofman IL, Taschner PE, Martin JJ, Philippart M, Andermann E, Andermann F, Mole SE, Gardiner RM, O'Rawe AM: Mutations in the palmitoyl-protein thioesterase gene (PPT; CLN1) causing juvenile neuronal ceroid lipofuscinosis with granular osmiophilic deposits. Hum Mol Genet. 1998 Feb;7(2):291-7. [PubMed Link Image]
  7. Das AK, Becerra CH, Yi W, Lu JY, Siakotos AN, Wisniewski KE, Hofmann SL: Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S. J Clin Invest. 1998 Jul 15;102(2):361-70. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 6373
Enzyme 44 Name Acid ceramidase precursor
Enzyme 44 Synonyms
  1. Acylsphingosine deacylase
  2. N-acylsphingosine amidohydrolase
  3. AC
  4. Putative 32 kDa heart protein
  5. PHP32[Contains: Acid ceramidase subunit alpha
  6. Acid ceramidase subunit beta]
Enzyme 44 Gene Name ASAH1
Enzyme 44 Protein Sequence >Acid ceramidase precursor
MPGRSCVALVLLAAAVSCAVAQHAPPWTEDCRKSTYPPSGPTYRGAVPWYTINLDLPPYK
RWHELMLDKAPMLKVIVNSLKNMINTFVPSGKVMQVVDEKLPGLLGNFPGPFEEEMKGIA
AVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITE
QLKPLTVNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLTLNERFSINGGYLGILEWI
LGKKDAMWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKE
SLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLST
KPVLNKLTVYTTLIDVTKGQFETYLRDCPDPCIGW
Enzyme 44 Number of Residues 395
Enzyme 44 Molecular Weight 44650
Enzyme 44 Theoretical pI 7.70
Enzyme 44 GO Classification Not Available
Enzyme 44 General Function Not Available
Enzyme 44 Specific Function Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid
Enzyme 44 Pathways
Enzyme 44 Reactions
  • N-acylsphingosine + H2O = a carboxylate + sphingosine
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • 1-21
Enzyme 44 Transmembrane Regions Not Available
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 1743867 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID Q13510 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name ASAH1_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >1188 bp
ATGCCGGGCCGGAGTTGCGTCGCCTTAGTCCTCCTGGCTGCCGCCGTCAGCTGTGCCGTC
GCGCAGCACGCGCCGCCGTGGACAGAGGACTGCAGAAAATCAACCTATCCTCCTTCAGGA
CCAACGTACAGAGGTGCAGTTCCATGGTACACCATAAATCTTGACTTACCACCCTACAAA
AGATGGCATGAATTGATGCTTGACAAGGCACCAATGCTAAAGGTTATAGTGAATTCTCTG
AAGAATATGATAAATACATTCGTGCCAAGTGGAAAAGTTATGCAGGTGGTGGATGAAAAA
TTGCCTGGCCTACTTGGCAACTTTCCTGGCCCTTTTGAAGAGGAAATGAAGGGTATTGCC
GCTGTTACTGATATACCTTTAGGAGAGATTATTTCATTCAATATTTTTTATGAATTATTT
ACCATTTGTACTTCAATAGTAGCAGAAGACAAAAAAGGTCATCTAATACATGGGAGAAAC
ATGGATTTTGGAGTATTTCTTGGGTGGAACATAAATAATGATACCTGGGTCATAACTGAG
CAACTAAAACCTTTAACAGTGAATTTGGATTTCCAAAGAAACAACAAAACTGTCTTCAAG
GCTTCAAGCTTTGCTGGCTATGTGGGCATGTTAACAGGATTCAAACCAGGACTGTTCAGT
CTTACACTGAATGAACGTTTCAGTATAAATGGTGGTTATCTGGGTATTCTAGAATGGATT
CTGGGAAAGAAAGATGCCATGTGGATAGGGTTCCTCACTAGAACAGTTCTGGAAAATAGC
ACAAGTTATGAAGAAGCCAAGAATTTATTGACCAAGACCAAGATATTGGCCCCAGCCTAC
TTTATCCTGGGAGGCAACCAGTCTGGGGAAGGTTGTGTGATTACACGAGACAGAAAGGAA
TCATTGGATGTATATGAACTCGATGCTAAGCAGGGTAGATGGTATGTGGTACAAACAAAT
TATGACCGTTGGAAACATCCCTTCTTCCTTGATGATCGCAGAACGCCTGCAAAGATGTGT
CTGAACCGCACCAGCCAAGAGAATATCTCATTTGAAACCATGTATGATGTCCTGTCAACA
AAACCTGTCCTCAACAAGCTGACCGTATACACAACCTTGATAGATGTTACCAAAGGTCAA
TTCGAAACTTACCTGCGGGACTGCCCTGACCCTTGTATAGGTTGGTGA
Enzyme 44 GenBank Gene ID U70063 Link Image
Enzyme 44 GeneCard ID ASAH1 Link Image
Enzyme 44 GenAtlas ID ASAH1 Link Image
Enzyme 44 HGNC ID HGNC:735 Link Image
Enzyme 44 Chromosome Location 8
Enzyme 44 Locus 8p22-p21.3
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Koch J, Gartner S, Li CM, Quintern LE, Bernardo K, Levran O, Schnabel D, Desnick RJ, Schuchman EH, Sandhoff K: Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification Of the first molecular lesion causing Farber disease. J Biol Chem. 1996 Dec 20;271(51):33110-5. [PubMed Link Image]
  2. Bernardo K, Hurwitz R, Zenk T, Desnick RJ, Ferlinz K, Schuchman EH, Sandhoff K: Purification, characterization, and biosynthesis of human acid ceramidase. J Biol Chem. 1995 May 12;270(19):11098-102. [PubMed Link Image]
  3. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 7657
Enzyme 45 Name Peroxisome proliferator-activated receptor gamma
Enzyme 45 Synonyms
  1. PPAR-gamma
Enzyme 45 Gene Name PPARG
Enzyme 45 Protein Sequence >Peroxisome proliferator-activated receptor gamma
MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSF
DIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKT
QLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNC
RIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLR
ALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQE
QSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLAS
LMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVII
LSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQL
LQVIKKTETDMSLHPLLQEIYKDLY
Enzyme 45 Number of Residues 505
Enzyme 45 Molecular Weight 57621
Enzyme 45 Theoretical pI 5.77
Enzyme 45 GO Classification
Function
  • DNA binding
  • binding
  • ligand-dependent nuclear receptor activity
  • nucleic acid binding
  • receptor activity
  • signal transducer activity
  • steroid hormone receptor activity
  • transcription factor activity
Process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 45 General Function Not Available
Enzyme 45 Specific Function Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 1711117 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID P37231 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name PPARG_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >1518 bp
ATGGGTGAAACTCTGGGAGATTCTCCTATTGACCCAGAAAGCGATTCCTTCACTGATACA
CTGTCTGCAAACATATCACAAGAAATGACCATGGTTGACACAGAGATGCCATTCTGGCCC
ACCAACTTTGGGATCAGCTCCGTGGATCTCTCCGTAATGGAAGACCACTCCCACTCCTTT
GATATCAAGCCCTTCACTACTGTTGACTTCTCCAGCATTTCTACTCCACATTACGAAGAC
ATTCCATTCACAAGAACAGATCCAGTGGTTGCAGATTACAAGTATGACCTGAAACTTCAA
GAGTACCAAAGTGCAATCAAAGTGGAGCCTGCATCTCCACCTTATTATTCTGAGAAGACT
CAGCTCTACAATAAGCCTCATGAAGAGCCTTCCAACTCCCTCATGGCAATTGAATGTCGT
GTCTGTGGAGATAAAGCTTCTGGATTTCACTATGGAGTTCATGCTTGTGAAGGATGCAAG
GGTTTCTTCCGGAGAACAATCAGATTGAAGCTTATCTATGACAGATGTGATCTTAACTGT
CGGATCCACAAAAAAAGTAGAAATAAATGTCAGTACTGTCGGTTTCAGAAATGCCTTGCA
GTGGGGATGTCTCATAATGCCATCAGGTTTGGGCGGATGCCACAGGCCGAGAAGGAGAAG
CTGTTGGCGGAGATCTCCAGTGATATCGACCAGCTGAATCCAGAGTCCGCTGACCTCCGG
GCCCTGGCAAAACATTTGTATGACTCATACATAAAGTCCTTCCCGCTGACCAAAGCAAAG
GCGAGGGCGATCTTGACAGGAAAGACAACAGACAAATCACCATTCGTTATCTATGACATG
AATTCCTTAATGATGGGAGAAGATAAAATCAAGTTCAAACACATCACCCCCCTGCAGGAG
CAGAGCAAAGAGGTGGCCATCCGCATCTTTCAGGGCTGCCAGTTTCGCTCCGTGGAGGCT
GTGCAGGAGATCACAGAGTATGCCAAAAGCATTCCTGGTTTTGTAAATCTTGACTTGAAC
GACCAAGTAACTCTCCTCAAATATGGAGTCCACGAGATCATTTACACAATGCTGGCCTCC
TTGATGAATAAAGATGGGGTTCTCATATCCGAGGGCCAAGGCTTCATGACAAGGGAGTTT
CTAAAGAGCCTGCGAAAGCCTTTTGGTGACTTTATGGAGCCCAAGTTTGAGTTTGCTGTG
AAGTTCAATGCACTGGAATTAGATGACAGCGACTTGGCAATATTTATTGCTGTCATTATT
CTCAGTGGAGACCGCCCAGGTTTGCTGAATGTGAAGCCCATTGAAGACATTCAAGACAAC
CTGCTACAAGCCCTGGAGCTCCAGCTGAAGCTGAACCACCCTGAGTCCTCACAGCTGTTT
GCCAAGCTGCTCCAGAAAATGACAGACCTCAGACAGATTGTCACGGAACACGTGCAGCTA
CTGCAGGTGATCAAGAAGACGGAGACAGACATGAGTCTTCACCCGCTCCTGCAGGAGATC
TACAAGGACTTGTACTAG
Enzyme 45 GenBank Gene ID U79012 Link Image
Enzyme 45 GeneCard ID PPARG Link Image
Enzyme 45 GenAtlas ID PPARG Link Image
Enzyme 45 HGNC ID HGNC:9236 Link Image
Enzyme 45 Chromosome Location 3
Enzyme 45 Locus 3p25
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Mukherjee R, Jow L, Croston GE, Paterniti JR Jr: Identification, characterization, and tissue distribution of human peroxisome proliferator-activated receptor (PPAR) isoforms PPARgamma2 versus PPARgamma1 and activation with retinoid X receptor agonists and antagonists. J Biol Chem. 1997 Mar 21;272(12):8071-6. [PubMed Link Image]
  2. Elbrecht A, Chen Y, Cullinan CA, Hayes N, Leibowitz M, Moller DE, Berger J: Molecular cloning, expression and characterization of human peroxisome proliferator activated receptors gamma 1 and gamma 2. Biochem Biophys Res Commun. 1996 Jul 16;224(2):431-7. [PubMed Link Image]
  3. Yanase T, Yashiro T, Takitani K, Kato S, Taniguchi S, Takayanagi R, Nawata H: Differential expression of PPAR gamma1 and gamma2 isoforms in human adipose tissue. Biochem Biophys Res Commun. 1997 Apr 17;233(2):320-4. [PubMed Link Image]
  4. Greene ME, Blumberg B, McBride OW, Yi HF, Kronquist K, Kwan K, Hsieh L, Greene G, Nimer SD: Isolation of the human peroxisome proliferator activated receptor gamma cDNA: expression in hematopoietic cells and chromosomal mapping. Gene Expr. 1995;4(4-5):281-99. [PubMed Link Image]
  5. Okazawa H, Mori H, Tamori Y, Araki S, Niki T, Masugi J, Kawanishi M, Kubota T, Shinoda H, Kasuga M: No coding mutations are detected in the peroxisome proliferator-activated receptor-gamma gene in Japanese patients with lipoatrophic diabetes. Diabetes. 1997 Nov;46(11):1904-6. [PubMed Link Image]
  6. Lambe KG, Tugwood JD: A human peroxisome-proliferator-activated receptor-gamma is activated by inducers of adipogenesis, including thiazolidinedione drugs. Eur J Biochem. 1996 Jul 1;239(1):1-7. [PubMed Link Image]
  7. Caira F, Antonson P, Pelto-Huikko M, Treuter E, Gustafsson JA: Cloning and characterization of RAP250, a novel nuclear receptor coactivator. J Biol Chem. 2000 Feb 25;275(8):5308-17. [PubMed Link Image]
  8. Shao W, Halachmi S, Brown M: ERAP140, a conserved tissue-specific nuclear receptor coactivator. Mol Cell Biol. 2002 May;22(10):3358-72. [PubMed Link Image]
  9. Gampe RT Jr, Montana VG, Lambert MH, Miller AB, Bledsoe RK, Milburn MV, Kliewer SA, Willson TM, Xu HE: Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol Cell. 2000 Mar;5(3):545-55. [PubMed Link Image]
  10. Yen CJ, Beamer BA, Negri C, Silver K, Brown KA, Yarnall DP, Burns DK, Roth J, Shuldiner AR: Molecular scanning of the human peroxisome proliferator activated receptor gamma (hPPAR gamma) gene in diabetic Caucasians: identification of a Pro12Ala PPAR gamma 2 missense mutation. Biochem Biophys Res Commun. 1997 Dec 18;241(2):270-4. [PubMed Link Image]
  11. Ristow M, Muller-Wieland D, Pfeiffer A, Krone W, Kahn CR: Obesity associated with a mutation in a genetic regulator of adipocyte differentiation. N Engl J Med. 1998 Oct 1;339(14):953-9. [PubMed Link Image]
  12. Hamann A, Munzberg H, Buttron P, Busing B, Hinney A, Mayer H, Siegfried W, Hebebrand J, Greten H: Missense variants in the human peroxisome proliferator-activated receptor-gamma2 gene in lean and obese subjects. Eur J Endocrinol. 1999 Jul;141(1):90-2. [PubMed Link Image]
  13. Sarraf P, Mueller E, Smith WM, Wright HM, Kum JB, Aaltonen LA, de la Chapelle A, Spiegelman BM, Eng C: Loss-of-function mutations in PPAR gamma associated with human colon cancer. Mol Cell. 1999 Jun;3(6):799-804. [PubMed Link Image]
  14. Barroso I, Gurnell M, Crowley VE, Agostini M, Schwabe JW, Soos MA, Maslen GL, Williams TD, Lewis H, Schafer AJ, Chatterjee VK, O'Rahilly S: Dominant negative mutations in human PPARgamma associated with severe insulin resistance, diabetes mellitus and hypertension. Nature. 1999 Dec 23-30;402(6764):880-3. [PubMed Link Image]
  15. Agarwal AK, Garg A: A novel heterozygous mutation in peroxisome proliferator-activated receptor-gamma gene in a patient with familial partial lipodystrophy. J Clin Endocrinol Metab. 2002 Jan;87(1):408-11. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 8375
Enzyme 46 Name Long-chain fatty acid transport protein 6
Enzyme 46 Synonyms
  1. Fatty acid transport protein 6
  2. FATP-6
  3. Very long-chain acyl-CoA synthetase homolog 1
  4. VLCSH1
  5. hVLCS-H1
  6. Fatty-acid-coenzyme A ligase, very long-chain 2
  7. Solute carrier family 27 member 6
Enzyme 46 Gene Name SLC27A6
Enzyme 46 Protein Sequence >Long-chain fatty acid transport protein 6
MLLSWLTVLGAGMVVLHFLQKLLFPYFWDDFWFVLKVVLIIIRLKKYEKRGELVTVLDKF
LSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVH
VWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVGADLLGTVEEILPSLSENISVW
GMKDSVPQGVISLKEKLSTSPDEPVPRSHHVVSLLKSTCLYIFTSGTTGLPKAAVISQLQ
VLRGSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDC
KKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFGNIKVCEL
YAATESSISFMNYTGRIGAIGRTNLFYKLLSTFDLIKYDFQKDEPMRNEQGWCIHVKKGE
PGLLISRVNAKNPFFGYAGPYKHTKDKLLCDVFKKGDVYLNTGDLIVQDQDNFLYFWDRT
GDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYEGRAGMASIILKPNTSLDLEK
VYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVEDGFNPLKISEPLYFMDNLKKS
YVLLTRELYDQIMLGEIKL
Enzyme 46 Number of Residues 619
Enzyme 46 Molecular Weight 70112
Enzyme 46 Theoretical pI 8.66
Enzyme 46 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 46 General Function Lipid transport and metabolism
Enzyme 46 Specific Function Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. Thought to function as the predominant fatty acid protein transporter in heart
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • 1-21
Enzyme 46 Transmembrane Regions
  • 22-42 119-139
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 4768275 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID Q9Y2P4 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name S27A6_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >1860 bp
ATGCTGCTGTCATGGCTAACAGTTCTAGGGGCTGGAATGGTCGTCCTGCACTTCTTGCAG
AAACTCCTGTTCCCTTACTTTTGGGATGACTTCTGGTTCGTGTTGAAGGTGGTGCTCATT
ATAATTCGGCTGAAGAAGTATGAAAAGAGAGGGGAGCTGGTGACTGTGCTGGATAAATTC
TTGAGTCATGCCAAAAGACAACCTCGGAAACCTTTCATCATCTATGAGGGAGACATCTAC
ACCTATCAGGATGTAGACAAAAGGAGCAGCAGAGTGGCCCATGTCTTCCTGAACCATTCC
TCTCTGAAAAAGGGGGACACGGTGGCTCTGCTGATGAGCAATGAGCCGGACTTCGTTCAC
GTGTGGTTCGGCCTCGCCAAGCTGGGCTGCGTGGTGGCCTTTCTCAACACCAACATTCGC
TCCAACTCCCTCCTGAATTGCATCCGCGCCTGTGGGCCCAGAGCCCTAGTGGTGGGCGCA
GATTTGCTTGGAACGGTAGAAGAAATCCTTCCAAGCCTCTCAGAAAATATCAGTGTTTGG
GGGATGAAAGATTCTGTTCCACAAGGTGTAATTTCACTCAAAGAAAAACTGAGCACCTCA
CCTGATGAGCCCGTGCCACGCAGCCACCATGTTGTCTCACTCCTCAAGTCTACTTGTCTT
TACATTTTTACCTCTGGAACAACAGGTCTACCAAAAGCAGCTGTGATTAGTCAGCTGCAG
GTTTTAAGGGGTTCTGCTGTCCTGTGGGCTTTTGGTTGTACTGCTCATGACATTGTTTAT
ATAACCCTTCCTCTGTATCATAGTTCAGCAGCTATCCTGGGAATTTCTGGATGTGTTGAG
TTGGGTGCCACTTGTGTGTTAAAGAAGAAATTTTCAGCAAGCCAGTTTTGGAGTGACTGC
AAGAAGTATGATGTGACTGTGTTTCAGTATATTGGAGAACTTTGTCGCTACCTTTGCAAA
CAATCTAAGAGAGAAGGAGAAAAGGATCATAAGGTGCGTTTGGCAATTGGAAATGGCATA
CGGAGTGATGTATGGAGAGAATTTTTAGACAGATTTGGAAATATAAAGGTGTGTGAACTT
TATGCAGCTACCGAATCAAGCATATCTTTCATGAACTACACTGGGAGAATTGGAGCAATT
GGGAGAACAAATTTGTTTTACAAACTTCTTTCCACTTTTGACTTAATAAAGTATGACTTT
CAGAAAGATGAACCCATGAGAAATGAGCAGGGTTGGTGTATTCATGTGAAAAAAGGAGAA
CCTGGACTTCTCATTTCTCGAGTGAATGCAAAAAATCCCTTCTTTGGCTATGCTGGGCCT
TATAAGCACACAAAAGACAAATTGCTTTGTGATGTTTTTAAGAAGGGAGATGTTTACCTT
AATACTGGAGACTTAATAGTCCAGGATCAGGACAATTTCCTTTATTTTTGGGACCGTACT
GGAGACACTTTCAGATGGAAAGGAGAAAATGTCGCAACCACTGAGGTTGCTGATGTTATT
GGAATGTTGGATTTCATACAGGAAGCAAACGTCTATGGTGTGGCTATATCAGGTTATGAA
GGAAGAGCAGGAATGGCTTCTATTATTTTAAAACCAAATACATCTTTAGATTTGGAAAAA
GTTTATGAACAAGTTGTAACATTTCTACCAGCTTATGCTTGTCCACGATTTTTAAGAATT
CAGGAAAAAATGGAAGCAACAGGAACATTCAAACTATTGAAGCATCAGTTGGTGGAAGAT
GGATTTAATCCACTGAAAATTTCTGAACCACTTTACTTCATGGATAACTTGAAAAAGTCT
TATGTTCTACTGACCAGGGAACTTTATGATCAAATAATGTTAGGGGAAATAAAACTTTAA
Enzyme 46 GenBank Gene ID AF064254 Link Image
Enzyme 46 GeneCard ID SLC27A6 Link Image
Enzyme 46 GenAtlas ID SLC27A6 Link Image
Enzyme 46 HGNC ID HGNC:11000 Link Image
Enzyme 46 Chromosome Location 5
Enzyme 46 Locus 5q23.3
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References Not Available
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 8493
Enzyme 47 Name Thioesterase domain containing 1
Enzyme 47 Synonyms Not Available
Enzyme 47 Gene Name THEDC1
Enzyme 47 Protein Sequence >Thioesterase domain containing 1
MERGDQPKRTRNENIFNCLYKNPEATFKLICFPWMGGGSTHFAKWGQDTHDLLEVHSLRL
PGRESRVEEPLENDISQLVDEVVCALQPVIQDKPFAFFGHSMGSYIAFRTALGLKENNQP
EPLHLFLSSATPVHSKAWHRIPKDDELSEEQISHYLMEFGGTPKHFAEAKEFVKQCSPII
RADLNIVRSCTSNVPSKAVLSCDLTCFVGSEDIAKDMEAWKDVTSGNAKIYQLPGGHFYL
LDPANEKLIKNYIIKCLEVSSISNF
Enzyme 47 Number of Residues 265
Enzyme 47 Molecular Weight 29931
Enzyme 47 Theoretical pI 6.17
Enzyme 47 GO Classification
Function
  • CoA hydrolase activity
  • acyl-CoA thioesterase II activity
  • acyl-CoA thioesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • thiolester hydrolase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 47 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 47 Specific Function Not Available
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals Not Available
Enzyme 47 Transmembrane Regions Not Available
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein Not Available
Enzyme 47 UniProtKB/Swiss-Prot ID Q5VUB6 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name Q5VUB6_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence Not Available
Enzyme 47 GenBank Gene ID AL590365 Link Image
Enzyme 47 GeneCard ID OLAH Link Image
Enzyme 47 GenAtlas ID OLAH Link Image
Enzyme 47 HGNC ID HGNC:25625 Link Image
Enzyme 47 Chromosome Location 10
Enzyme 47 Locus 10p13
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References Not Available
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 8676
Enzyme 48 Name Long-chain fatty acid transport protein 3
Enzyme 48 Synonyms
  1. Fatty acid transport protein 3
  2. FATP-3
  3. Very long-chain acyl-CoA synthetase homolog 3
  4. VLCS-3
  5. Solute carrier family 27 member 3
Enzyme 48 Gene Name SLC27A3
Enzyme 48 Protein Sequence >Long-chain fatty acid transport protein 3
MAALLLLPLLLLLPLLLLKLHLWPQLRWLPADLAFAVRALCCKRALRARALAAAAADPEG
PEGGCSLAWRLAELAQQRAAHTFLIHGSRRFSYSEAERESNRAARAFLRALGWDWGPDGG
DSGEGSAGEGERAAPGAGDAAAGSGAEFAGGDGAARGGGAAAPLSPGATVALLLPAGPEF
LWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLEPDLPALRAMGL
HLWAAGPGTHPAGISDLLAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARI
SHLKILQCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQF
WEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLRPDTWERFVRRFGPLQ
VLETYGLTEGNVATINYTGQRGAVGRASWLYKHIFPFSLIRYDVTTGEPIRDPQGHCMAT
SPGEPGLLVAPVSQQSPFLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRF
HDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHEGRAGMAALVLRPPHAL
DLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGFDPSTLSDPLYVLDQ
AVGAYLPLTTARYSALLAGNLRI
Enzyme 48 Number of Residues 683
Enzyme 48 Molecular Weight 73551
Enzyme 48 Theoretical pI 7.09
Enzyme 48 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 48 General Function Lipid transport and metabolism
Enzyme 48 Specific Function Has acyl-CoA ligase activity for long-chain and very- long-chain fatty acids. Does not exhibit fatty acid transport activity
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • 1-28
Enzyme 48 Transmembrane Regions
  • 3-23 322-342
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 57161863 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID Q5K4L6 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name S27A3_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >90 bp
ATGGTACCTTCCCTTAACGGGAAAACGAGAAATATTGAGGGGAAGATGGACTGCGATCCA
AACGCCCTGGCTCTCAGGCCTGGACTCTAG
Enzyme 48 GenBank Gene ID AJ577572 Link Image
Enzyme 48 GeneCard ID SLC27A3 Link Image
Enzyme 48 GenAtlas ID SLC27A3 Link Image
Enzyme 48 HGNC ID HGNC:10997 Link Image
Enzyme 48 Chromosome Location 1
Enzyme 48 Locus 1q21.3
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 8715
Enzyme 49 Name Patatin-like phospholipase domain-containing protein 4
Enzyme 49 Synonyms
  1. Protein GS2
Enzyme 49 Gene Name PNPLA4
Enzyme 49 Protein Sequence >Patatin-like phospholipase domain-containing protein 4
MKHINLSFAACGFLGIYHLGAASALCRHGKKLVKDVKAFAGASAGSLVASVLLTAPEKIE
ECNQFTYKFAEEIRRQSFGAVTPGYDFMARLRSGMESILPPSAHELAQNRLHVSITNAKT
RENHLVSTFSSREDLIKVLLASSFVPIYAGLKLVEYKGQKWVDGGLTNALPILPVGRTVT
ISPFSGRLDISPQDKGQLDLYVNIAKQDIMLSLANLVRLNQALFPPSKRKMESLYQCGFD
DTVKFLLKENWFE
Enzyme 49 Number of Residues 253
Enzyme 49 Molecular Weight 27981
Enzyme 49 Theoretical pI 9.54
Enzyme 49 GO Classification
Function
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 49 General Function Not Available
Enzyme 49 Specific Function Not Available
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • 1-24
Enzyme 49 Transmembrane Regions Not Available
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 458226 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID P41247 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name PLPL4_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >762 bp
ATGAAGCACATCAACCTATCATTTGCAGCGTGTGGATTTCTGGGCATTTACCACTTGGGG
GCAGCATCTGCACTTTGCAGACATGGCAAAAAACTTGTGAAGGATGTCAAAGCCTTCGCT
GGGGCGTCTGCGGGATCGTTGGTTGCTTCTGTTCTGCTAACAGCACCAGAAAAAATAGAG
GAATGTAACCAATTTACCTACAAGTTTGCCGAAGAAATCAGAAGGCAGTCTTTCGGGGCA
GTAACGCCCGGTTATGACTTCATGGCCCGACTAAGAAGTGGGATGGAGTCGATTCTTCCT
CCCAGCGCTCACGAGCTGGCCCAGAACCGACTGCACGTATCCATCACCAACGCCAAAACC
AGAGAAAATCACTTAGTCTCCACTTTTTCCTCCAGGGAGGACCTCATTAAGGTCCTCCTA
GCCAGCAGTTTTGTGCCCATTTATGCAGGACTGAAGCTAGTGGAATACAAAGGGCAGAAG
TGGGTGGACGGAGGCCTCACCAACGCTCTTCCCATCCTGCCCGTCGGCCGGACAGTAACC
ATCTCCCCCTTCAGTGGACGACTGGACATCTCCCCGCAGGACAAAGGGCAGCTAGATCTG
TATGTTAATATCGCCAAGCAGGATATCATGTTGTCCCTGGCAAACCTGGTGAGACTCAAC
CAAGCCCTTTTTCCCCCAAGCAAGAGGAAAATGGAATCTTTGTATCAGTGTGGTTTTGAT
GACACTGTTAAGTTTTTACTTAAAGAAAATTGGTTTGAATAA
Enzyme 49 GenBank Gene ID U03886 Link Image
Enzyme 49 GeneCard ID PNPLA4 Link Image
Enzyme 49 GenAtlas ID PNPLA4 Link Image
Enzyme 49 HGNC ID HGNC:24887 Link Image
Enzyme 49 Chromosome Location X
Enzyme 49 Locus Xp22.3
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Lee WC, Salido E, Yen PH: Isolation of a new gene GS2 (DXS1283E) from a CpG island between STS and KAL1 on Xp22.3. Genomics. 1994 Jul 15;22(2):372-6. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 8735
Enzyme 50 Name Long-chain fatty acid transport protein 1
Enzyme 50 Synonyms
  1. Fatty acid transport protein 1
  2. FATP-1
  3. Solute carrier family 27 member 1
Enzyme 50 Gene Name SLC27A1
Enzyme 50 Protein Sequence >Long-chain fatty acid transport protein 1
MRAPGAGAASVVSLALLWLLGLPWTWSAAAALGVYVGSGGWRFLRIVCKTARRDLFGLSV
LIRVRLELRRHQRAGHTIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLF
RQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI
FGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPSKGM
DDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIG
VGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRL
AVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHVYPIR
LVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRFDGYVSESATSKKIAHSV
FSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVY
GVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQ
KTRLQREGFDPRQTSDRLFFLDLKQGHYLPLNEAVYTRICSGAFAL
Enzyme 50 Number of Residues 646
Enzyme 50 Molecular Weight 71109
Enzyme 50 Theoretical pI 8.63
Enzyme 50 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 50 General Function Lipid transport and metabolism
Enzyme 50 Specific Function Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. The LFCA import appears to be hormone-regulated in a tissue-specific manner. In adipocytes, but not myocytes, insulin induces a rapid translocation of FATP1 from intracellular compartments to the plasma membrane, paralleled by increased LFCA uptake. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane- associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LFCA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • 1-31
Enzyme 50 Transmembrane Regions
  • 14-34
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 37590807 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q6PCB7 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name S27A1_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >1941 bp
ATGCGGGCTCCGGGTGCGGGCGCGGCCTCGGTGGTCTCGCTGGCGCTGTTGTGGCTGCTG
GGGCTGCCGTGGACCTGGAGCGCGGCAGCGGCGCTCGGCGTGTACGTGGGCAGCGGCGGC
TGGCGCTTCCTGCGCATCGTCTGCAAGACCGCGAGGCGAGACCTCTTCGGTCTCTCTGTG
CTGATCCGCGTGCGCCTGGAGCTGCGGCGGCACCAGCGTGCCGGCCACACCATCCCGCGC
ATCTTTCAGGCGGTAGTGCAGCGACAGCCCGAGCGCCTGGCGCTGGTGGATGCCGGGACC
GGCGAGTGCTGGACCTTTGCGCAGCTGGACGCCTACTCCAATGCGGTAGCCAACCTCTTC
CGCCAGCTGGGCTTCGCGCCGGGCGACGTGGTGGCCATCTTCCTGGAGGGCCGGCCGGAG
TTCGTGGGGCTGTGGCTGGGCCTGGCCAAGGCGGGCATGGAGGCCGCGCTGCTCAACGTG
AACCTGCGGCGCGAGCCCCTGGCCTTCTGCCTGGGCACCTCGGGCGCTAAGGCCCTGATC
TTTGGAGGAGAAATGGTGGCGGCGGTGGCCGAAGTGAGCGGGCATCTGGGGAAAAGTTTG
ATCAAGTTCTGCTCTGGAGACTTGGGGCCCGAGGGCATCTTGCCGGACACCCACCTCCTG
GACCCGCTGCTGAAGGAGGCCTCTACTGCCCCCTTGGCACAGATCCCCAGCAAGGGCATG
GACGATCGTCTTTTCTACATCTACACGTCGGGGACCACCGGGCTGCCCAAGGCTGCCATT
GTCGTGCACAGCAGGTACTACCGCATGGCAGCCTTCGGCCACCACGCCTACCGCATGCAG
GCGGCTGACGTGCTCTATGACTGCCTGCCCCTGTACCACTCGGCAGGAAACATCATCGGC
GTGGGGCAGTGTCTCATCTATGGGCTGACAGTCGTCCTCCGCAAGAAATTCTCGGCCAGC
CGCTTCTGGGACGACTGCATCAAGTACAACTGCACGGTGGTTCAGTACATCGGGGAGATC
TGCCGCTACCTGCTGAAGCAGCCGGTGCGCGAGGCGGAGAGGCGACACCGCGTGCGCCTG
GCGGTGGGGAACGGGCTGCGTCCTGCCATCTGGGAGGAGTTCACGGAGCGCTTCGGCGTA
CGCCAAATCGGGGAGTTCTACGGCGCCACCGAGTGCAACTGCAGCATTGCCAACATGGAC
GGCAAGGTCGGCTCCTGTGGTTTCAACAGCCGCATCCTGCCCCACGTGTACCCCATCCGG
CTGGTGAAGGTCAATGAGGACACAATGGAGCTGCTGCGGGATGCCCAGGGCCTCTGCATC
CCCTGCCAGGCCGGGGAGCCTGGCCTCCTTGTGGGTCAGATCAACCAACAGGACCCGCTG
CGCCGCTTCGATGGCTATGTCAGCGAGAGCGCCACCAGCAAGAAGATCGCCCACAGCGTC
TTCAGCAAGGGCGACAGCGCCTACCTCTCAGGTGACGTGCTAGTGATGGATGAGCTGGGC
TACATGTACTTCCGGGACCGTAGCGGGGACACCTTCCGCTGGCGAGGGGAGAACGTCTCC
ACCACCGAGGTGGAGGGCGTGCTGAGCCGCCTGCTGGGCCAGACAGACGTGGCCGTCTAT
GGGGTGGCTGTTCCAGGAGTGGAGGGTAAGGCAGGGATGGCGGCCGTCGCAGACCCCCAC
AGCCTGCTGGACCCCAACGCGATATACCAGGAGCTGCAGAAGGTGCTGGCACCCTATGCC
CGGCCCATCTTCCTGCGCCTCCTGCCCCAGGTGGACACCACAGGCACCTTCAAGATCCAG
AAGACGAGGCTGCAGCGAGAGGGCTTTGACCCACGCCAGACCTCAGACCGGCTCTTCTTC
CTGGACCTGAAGCAGGGCCACTACCTGCCCTTAAATGAGGCAGTCTACACTCGCATCTGC
TCGGGCGCCTTCGCCCTCTGA
Enzyme 50 GenBank Gene ID BC059399 Link Image
Enzyme 50 GeneCard ID SLC27A1 Link Image
Enzyme 50 GenAtlas ID SLC27A1 Link Image
Enzyme 50 HGNC ID HGNC:10995 Link Image
Enzyme 50 Chromosome Location 19
Enzyme 50 Locus 19p13.11
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Hatch GM, Smith AJ, Xu FY, Hall AM, Bernlohr DA: FATP1 channels exogenous FA into 1,2,3-triacyl-sn-glycerol and down-regulates sphingomyelin and cholesterol metabolism in growing 293 cells. J Lipid Res. 2002 Sep;43(9):1380-9. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 12492
Enzyme 51 Name Long-chain fatty acid transport protein 4
Enzyme 51 Synonyms
  1. Fatty acid transport protein 4
  2. FATP-4
  3. Solute carrier family 27 member 4
Enzyme 51 Gene Name SLC27A4
Enzyme 51 Protein Sequence >Long-chain fatty acid transport protein 4
MLLGASLVGVLLFSKLVLKLPWTQVGFSLLFLYLGSGGWRFIRVFIKTIRRDIFGGLVLL
KVKAKVRQCLQERRTVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQA
RGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFG
SEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDK
LFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQ
CLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALG
NGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVR
VNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVFKK
GDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVE
VPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTE
LRKEGFDPAIVKDPLFYLDAQKGRYVPLDQEAYSRIQAGEEKL
Enzyme 51 Number of Residues 643
Enzyme 51 Molecular Weight 72065
Enzyme 51 Theoretical pI Not Available
Enzyme 51 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 51 General Function Lipid transport and metabolism
Enzyme 51 Specific Function Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. Appears to be the principal fatty acid transporter in small intestinal enterocytes. Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions
  • Hexadecanoate (n-C16:0)[c] + Sodium[c] <==> Hexadecanoate (n-C16:0)[e] + Sodium[e]
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • 20-42 139-156
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 4206376 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID Q6P1M0 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name S27A4_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence Not Available
Enzyme 51 GenBank Gene ID AF055899 Link Image
Enzyme 51 GeneCard ID Not Available
Enzyme 51 GenAtlas ID SLC27A4 Link Image
Enzyme 51 HGNC ID HGNC:10998 Link Image
Enzyme 51 Chromosome Location Not Available
Enzyme 51 Locus Not Available
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Fitscher BA, Riedel HD, Young KC, Stremmel W: Tissue distribution and cDNA cloning of a human fatty acid transport protein (hsFATP4). Biochim Biophys Acta. 1998 Dec 22;1443(3):381-5. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 12921
Enzyme 52 Name Full-length cDNA clone CS0DM001YM08 of Fetal liver of Homo sapiens
Enzyme 52 Synonyms
  1. human
  2. HCG23215, isoform CRA_b
Enzyme 52 Gene Name Not Available
Enzyme 52 Protein Sequence >Full-length cDNA clone CS0DM001YM08 of Fetal liver of Homo sapiens
MAGPSPPLRAGVGRRLLGVAHPDLRPCLCGELQVEGGPGPVPGMLRTCYVRSPWRRGPSS
ARGEQSGSGHLEQEEVQSGSLLFRLLLFLSRSPASRNQRILYTVLECQPLFDSSDMTIAE
WVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSD
GRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADI
TINRELVRKVDGKAGLVVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGN
GPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTDYAAGMAMAGAGVISGFDMTSEAALA
KLSYVLGQPGLSLDVRKELLTKDLRGEMTPPSVEERRPSLQGNTLGGGVSWLLSLSGSQE
ADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAA
Enzyme 52 Number of Residues 469
Enzyme 52 Molecular Weight 50186
Enzyme 52 Theoretical pI 6.83
Enzyme 52 GO Classification
Function
  • asparaginase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
Enzyme 52 General Function Amino acid transport and metabolism
Enzyme 52 Specific Function Not Available
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 28193178 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID Q86U10 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name Q86U10_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence Not Available
Enzyme 52 GenBank Gene ID BX247999 Link Image
Enzyme 52 GeneCard ID Q86U10 Link Image
Enzyme 52 GenAtlas ID Not Available
Enzyme 52 HGNC ID Not Available
Enzyme 52 Chromosome Location Not Available
Enzyme 52 Locus Not Available
Enzyme 52 SNPs Not Available
Enzyme 52 General References Not Available
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 12922
Enzyme 53 Name Phospholipase B1
Enzyme 53 Synonyms Not Available
Enzyme 53 Gene Name PLB1
Enzyme 53 Protein Sequence >Phospholipase B1
MEPAGEKDEPLSVKHGRPMKCPSQESPYLFSYRNSNYLTRLQKPQDKLEVREGAEIRCPD
KDPSDTVPTSVHRLKPADINVIGALGDSLTAGNGAGSTPGNVLDVLTQYRGLSWSVGGDE
NIGTVTTLANILREFNPSLKGFSVGTGKETSPNAFLNQAVAGGRAEDLPVQARRLVDLMK
NDTRIHFQEDWKIITLFIGGNDLCDFCNDLVHYSPQNFTDNIGKALDILHAEVPRAFVNL
VTVLEIVNLRELYQEKKVYCPRMILRSLCPCVLKFDDNSTELATLIEFNKKFQEKTHQLI
ESGRYDTREDFTVVVQPFFENVDMPKTSEGLPDNSFFAPDCFHFSSKSHSRAASALWNNM
LEPVGQKTTRHKFENKINITCPNQVQPFLRTYKNSMQGHGTWLPCRDRAPSALHPTSVHA
LRPADIQVVAALGDSLTAGNGIGSKPDDLPDVTTQYRGLSYRESKPGFLSDSWVSKSNRK
CTRKAPNP
Enzyme 53 Number of Residues 488
Enzyme 53 Molecular Weight 54342
Enzyme 53 Theoretical pI 7.29
Enzyme 53 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 53 General Function Not Available
Enzyme 53 Specific Function Not Available
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 40674028 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID