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Human Metabolome Database Version 2.5

 

Showing metabocard for Eicosapentaenoic acid (HMDB01999)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:31
Update Date 2009-11-18 17:45:41
Accession Number HMDB01999
Secondary Accession Numbers Not Available
Common Name Eicosapentaenoic acid
Description Eicosapentaenoic acid (EPA or also icosapentaenoic acid) is an important polyunsaturated fatty acid found in fish oils. It serves as the precursor for the prostaglandin-3 and thromboxane-3 families. A diet rich in eicosapentaenoic acid lowers serum lipid concentration, reduces incidence of cardiovascular disorders, prevents platelet aggregation, and inhibits arachidonic acid conversion into the thromboxane-2 and prostaglandin-2 families. Eicosapentaenoic acid is an omega-3 fatty acid. In physiological literature, it is given the name 20:5(n-3). Its systematic chemical name is all-cis-5,8,11,14,17-icosapentaenoic acid. It also has the trivial name timnodonic acid. Chemically, EPA is a carboxylic acid with a 20-carbon chain and five cis double bonds; the first double bond is located at the third carbon from the omega end. Because of the presence of double bonds, EPS is a polyunsaturated fatty acid. Metabolically it acts as a precursor for prostaglandin-3 (which inhibits platelet aggregation), thromboxane-3 and leukotriene-5 groups. It is found in fish oils of cod liver, herring, mackerel, salmon, menhaden and sardine. It is also found in human breast milk. -- Wikipedia
Synonyms
  1. (5Z,8Z,11Z,14Z,17Z)-Eicosapentaenoate
  2. 5,8,11,14,17-Eicosapentaenoate
  3. 5,8,11,14,17-Eicosapentaenoic acid
  4. 5,8,11,14,17-Icosapentaenoate
  5. 5,8,11,14,17-Icosapentaenoic acid
  6. 5Z,8Z,11Z,14Z,17Z-Eicosapentaenoate
  7. 5Z,8Z,11Z,14Z,17Z-Eicosapentaenoic acid
  8. EPA
  9. Eicosapentaenoate
  10. Icosapent
  11. Icosapentaenoate
  12. Icosapentaenoic acid
  13. Icosapento
  14. Icosapentum
  15. Timnodonate
  16. Timnodonic acid
  17. all-cis-icosapentaenoate
  18. all-cis-icosapentaenoic acid
  19. cis-5,8,11,14,17-Eicosapentaenoate
  20. cis-5,8,11,14,17-Eicosapentaenoic acid
  21. (5Z,8Z,11Z,14Z,17Z)-Eicosapentaenoic acid
  22. Eicosapentaenoic acid
Chemical IUPAC Name (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoic acid
Chemical Formula C20H30O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Fatty acids
Class
  • Eicosanoids
Sub Class
  • Eicosapolyenoic acids
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • alkene
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 302.451
Monoisotopic Molecular Weight 302.224579
Isomeric SMILES CCC=C/CC=C/CC=C/CC=C/CC=C/CCCC(O)=O
Canonical SMILES CCC=CCC=CCC=CCC=CCC=CCCCC(O)=O
KEGG Compound ID C06428 Link Image
BioCyc ID CPD-6941 Link Image
BiGG ID 2218016 Link Image
Wikipedia Link Eicosapentaenoic acid Link Image
NuGOwiki Link HMDB01999 Link Image
Metagene Link HMDB01999 Link Image
METLIN ID 6423 Link Image
PubChem Compound 446284 Link Image
PubChem Substance 631225 Link Image
ChEBI ID 28364 Link Image
CAS Registry Number 10417-94-4
InChI Identifier InChI=1/C20H30O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-18-19-20(21)22/h3-4,6-7,9-10,12-13,15-16H,2,5,8,11,14,17-19H2,1H3,(H,21,22)/b4-3-,7-6-,10-9-,13-12-,16-15-
Synthesis Reference Sandri, Jacqueline; Viala, Jacques. Syntheses of all-(Z)-5,8,11,14,17-Eicosapentaenoic Acid and all-(Z)-4,7,10,13,16,19-Docosahexaenoic Acid from (Z)-1,1,6,6-tetraisopropoxy-3-hexene. Journal of Organic Chemistry (1995), 60(20), 6627-30.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.89e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 6.53 [Predicted by ALOGPS]; 6.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
Biofluid Location
  • Blood
Tissue Location
Tissue References
Adipose Tissue
Epidermis
Erythrocyte
Fibroblasts
Neutrophil
Platelet
Skeletal Muscle
Concentrations (Normal)
Biofluid Blood
Value 2100.0 +/- 990.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information 5 hours after EPA meal
Comments 17 healthy men, plasma EPA concentration , 5 hours after EPA meal (5 g EPA plus high-oleic sunflower oil
References
  • Hall WL, Sanders KA, Sanders TA, Chowienczyk PJ: A high-fat meal enriched with eicosapentaenoic acid reduces postprandial arterial stiffness measured by digital volume pulse analysis in healthy men. J Nutr. 2008 Feb;138(2):287-91. [PubMed Link Image]
Biofluid Blood
Value 0.401 +/- 0.068 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 Blood
Value 270 +/- 160 uM
Age Adult:>18 yrs old
Sex Male
Patient information Placebo meal
Comments 17 healthy men, plasma EPA concentration , 1 hour after placebo meal (high-oleic sunflower oil with no added EPA)
References
  • Hall WL, Sanders KA, Sanders TA, Chowienczyk PJ: A high-fat meal enriched with eicosapentaenoic acid reduces postprandial arterial stiffness measured by digital volume pulse analysis in healthy men. J Nutr. 2008 Feb;138(2):287-91. [PubMed Link Image]
Biofluid Blood
Value 11.0 +/- 8.3 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Biofluid Blood
Value 11.1 +/- 9.5 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Biofluid Blood
Value 10.8 +/- 6.2 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments n=52
References
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 11.0 +/- 7.3 uM
Age Adult:>18 yrs old
Sex Both
Condition Hypertension
Comments n=109 Essential hypertension
References
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Biofluid Blood
Value 10.6 +/- 7.2 uM
Age Adult:>18 yrs old
Sex Male
Condition Essential hypertension
Comments n=75
References
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Biofluid Blood
Value 11.9 +/- 7.6 uM
Age Adult:>18 yrs old
Sex Female
Condition Essential hypertension
Comments Not Available
References
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Associated Disorders
Condition References
Essential hypertension
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Hypertension
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Alpha Linolenic Acid and Linoleic Acid Metabolism SMP00018 Link Image map00592 Link Image
General References
  1. Hafstrom I, Ringertz B, Gyllenhammar H, Palmblad J, Harms-Ringdahl M: Effects of fasting on disease activity, neutrophil function, fatty acid composition, and leukotriene biosynthesis in patients with rheumatoid arthritis. Arthritis Rheum. 1988 May;31(5):585-92. [PubMed Link Image]
  2. Woodman RJ, Mori TA, Burke V, Puddey IB, Barden A, Watts GF, Beilin LJ: Effects of purified eicosapentaenoic acid and docosahexaenoic acid on platelet, fibrinolytic and vascular function in hypertensive type 2 diabetic patients. Atherosclerosis. 2003 Jan;166(1):85-93. [PubMed Link Image]
  3. Sipka S, Dey I, Buda C, Csongor J, Szegedi G, Farkas T: The mechanism of inhibitory effect of eicosapentaenoic acid on phagocytic activity and chemotaxis of human neutrophil granulocytes. Clin Immunol Immunopathol. 1996 Jun;79(3):224-8. [PubMed Link Image]
  4. Miwa H, Yamamoto M, Futata T, Kan K, Asano T: Thin-layer chromatography and high-performance liquid chromatography for the assay of fatty acid compositions of individual phospholipids in platelets from non-insulin-dependent diabetes mellitus patients: effect of eicosapentaenoic acid ethyl ester administration. J Chromatogr B Biomed Appl. 1996 Mar 3;677(2):217-23. [PubMed Link Image]
  5. Kim HH, Shin CM, Park CH, Kim KH, Cho KH, Eun HC, Chung JH: Eicosapentaenoic acid inhibits UV-induced MMP-1 expression in human dermal fibroblasts. J Lipid Res. 2005 Aug;46(8):1712-20. Epub 2005 Jun 1. [PubMed Link Image]
  6. Gillis RC, Daley BJ, Enderson BL, Karlstad MD: Eicosapentaenoic acid and gamma-linolenic acid induce apoptosis in HL-60 cells. J Surg Res. 2002 Sep;107(1):145-53. [PubMed Link Image]
  7. Hino K, Murakami Y, Nagai A, Kitase A, Hara Y, Furutani T, Ren F, Yamaguchi Y, Yutoku K, Yamashita S, Okuda M, Okita M, Okita K: Alpha-tocopherol [corrected] and ascorbic acid attenuates the ribavirin [corrected] induced decrease of eicosapentaenoic acid in erythrocyte membrane in chronic hepatitis C patients. J Gastroenterol Hepatol. 2006 Aug;21(8):1269-75. [PubMed Link Image]
  8. Takenaga M, Hirai A, Terano T, Tamura Y, Kitagawa H, Yoshida S: Comparison of the in vitro effect of eicosapentaenoic acid (EPA)-derived lipoxygenase metabolites on human platelet function with those of arachidonic acid. Thromb Res. 1986 Feb 1;41(3):373-84. [PubMed Link Image]
  9. Hereliuk VI: [The role of arachidonic and eicosapentaenoic acid lipoxygenase products in the pathogenesis of generalized parodontosis] Fiziol Zh. 2000;46(6):112-5. [PubMed Link Image]
  10. Aas V, Rokling-Andersen MH, Kase ET, Thoresen GH, Rustan AC: Eicosapentaenoic acid (20:5 n-3) increases fatty acid and glucose uptake in cultured human skeletal muscle cells. J Lipid Res. 2006 Feb;47(2):366-74. Epub 2005 Nov 21. [PubMed Link Image]
  11. Kim HH, Cho S, Lee S, Kim KH, Cho KH, Eun HC, Chung JH: Photoprotective and anti-skin-aging effects of eicosapentaenoic acid in human skin in vivo. J Lipid Res. 2006 May;47(5):921-30. Epub 2006 Feb 7. [PubMed Link Image]
  12. Herrmann W, Beitz J: [Decreasing atherogenic risks by an eicosapentaenoic acid-rich diet] Z Gesamte Inn Med. 1987 Mar 1;42(5):117-22. [PubMed Link Image]
  13. Ide T, Okamura T, Kumashiro R, Koga Y, Hino T, Hisamochi A, Ogata K, Tanaka K, Kuwahara R, Seki R, Sata M: A pilot study of eicosapentaenoic acid therapy for ribavirin-related anemia in patients with chronic hepatitis C. Int J Mol Med. 2003 Jun;11(6):729-32. [PubMed Link Image]
  14. Francois CA, Connor SL, Bolewicz LC, Connor WE: Supplementing lactating women with flaxseed oil does not increase docosahexaenoic acid in their milk. Am J Clin Nutr. 2003 Jan;77(1):226-33. [PubMed Link Image]
  15. Dunstan JA, Roper J, Mitoulas L, Hartmann PE, Simmer K, Prescott SL: The effect of supplementation with fish oil during pregnancy on breast milk immunoglobulin A, soluble CD14, cytokine levels and fatty acid composition. Clin Exp Allergy. 2004 Aug;34(8):1237-42. [PubMed Link Image]
  16. Luostarinen R, Saldeen T: Dietary fish oil decreases superoxide generation by human neutrophils: relation to cyclooxygenase pathway and lysosomal enzyme release. Prostaglandins Leukot Essent Fatty Acids. 1996 Sep;55(3):167-72. [PubMed Link Image]
  17. Calzada C, Vericel E, Lagarde M: Lower levels of lipid peroxidation in human platelets incubated with eicosapentaenoic acid. Biochim Biophys Acta. 1992 Jul 29;1127(2):147-52. [PubMed Link Image]
  18. Lagarde M, Croset M, Vericel E, Calzada C: Effects of small concentrations of eicosapentaenoic acid on platelets. J Intern Med Suppl. 1989;731:177-9. [PubMed Link Image]
  19. Wikipedia Link Image
Metabolic Enzymes
  1. Bile acid CoA:amino acid N-acyltransferase
  2. Cytosolic acyl coenzyme A thioester hydrolase
  3. Acyl-coenzyme A thioesterase 2
  4. Acyl-coenzyme A thioesterase 8
  5. BC269730_2
  6. Acyl-CoA thioesterase 4
Enzyme 1 [top]
Enzyme 1 ID 5821
Enzyme 1 Name Bile acid CoA:amino acid N-acyltransferase
Enzyme 1 Synonyms
  1. BAT
  2. BACAT
  3. Glycine N-choloyltransferase
  4. Long-chain fatty-acyl-CoA hydrolase
Enzyme 1 Gene Name BAAT
Enzyme 1 Protein Sequence >Bile acid CoA:amino acid N-acyltransferase
MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDL
NHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVAS
APKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASL
LASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQI
GLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFE
TTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGA
GHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL
Enzyme 1 Number of Residues 418
Enzyme 1 Molecular Weight 46300
Enzyme 1 Theoretical pI 7.00
Enzyme 1 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 1 General Function Not Available
Enzyme 1 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 1 Pathways
Enzyme 1 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 532505 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q14032 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name BAAT_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID L34081 Link Image
Enzyme 1 GeneCard ID BAAT Link Image
Enzyme 1 GenAtlas ID BAAT Link Image
Enzyme 1 HGNC ID HGNC:932 Link Image
Enzyme 1 Chromosome Location 9
Enzyme 1 Locus 9q22.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6335
Enzyme 2 Name Cytosolic acyl coenzyme A thioester hydrolase
Enzyme 2 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 2 Gene Name ACOT7
Enzyme 2 Protein Sequence >Cytosolic acyl coenzyme A thioester hydrolase
MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIM
RPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGE
VAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVV
YSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCT
LHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTS
NKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEE
GKGRYLQMKAKRQGHAEPQP
Enzyme 2 Number of Residues 380
Enzyme 2 Molecular Weight 41797
Enzyme 2 Theoretical pI 8.66
Enzyme 2 GO Classification
Function
  • catalytic activity
Process
Component
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 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 2 Pathways Not Available
Enzyme 2 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-19
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 2780414 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O00154 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name BACH_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1017 bp
ATGTCGGGCCCAGACGTCGAGACGCCGTCCGCCATCCAGATCTGCCGGATCATGCGGCCA
GATGATGCCAACGTGGCCGGCAATGTCCACGGGGGGACCATCCTGAAGATGATCGAGGAG
GCAGGCGCCATCATCAGCACCCGGCATTGCAACAGCCAGAACGGGGAGCGCTGTGTGGCC
GCCCTGGCTCGTGTCGAGCGCACCGACTTCCTGTCTCCCATGTGCATCGGTGAGGTGGCG
CATGTCAGCGCGGAGATCACCTACACCTCCAAGCACTCTGTGGAGGTGCAGGTCAACGTG
ATGTCCGAAAACATCCTCACAGGTGCCAAAAAGCTGACCAATAAGGCCACCCTGTGGTAT
GTGCCCCTGTCGCTGAAGAATGTGGACAAGGTCCTCGAGGTGCCTCCTGTTGTGTATTCC
CGGCAGGAGCAGGAGGAGGAGGGCCGGAAGCGGTATGAAGCCCAGAAGCTGGAGCGCATG
GAGACCAAGTGGAGGAACGGGGACATCGTCCAGCCAGTCCTCAACCCAGAGCCGAACACT
GTCAGCTACAGCCAGTCCAGCTTGATCCACCTGGTGGGGCCTTCAGACTGCACCCTGCAC
GGCTTTGTGCACGGAGGTGTGACCATGAAGCTCATGGATGAGGTCGCCGGGATCGTGGCT
GCACGCCACTGCAAGACCAACATCGTCACAGCTTCCGTGGACGCCATTAATTTTCATGAC
AAGATCAGAAAAGGCTGCGTCATCACCATCTCGGGACGCATGACCTTCACGAGCAATAAG
TCCATGGAGATCGAGGTGTTGGTGGACGCCGACCCTGTTGTGGACAGCTCTCAGAAGCGC
TACCGGGCCGCCAGTGCCTTCTTCACCTACGTGTCGCTGAGCCAGGAAGGCAGGTCGCTG
CCTGTGCCCCAGCTGGTGCCCGAGACCGAGGACGAGAAGAAGCGCTTTGAGGAAGGCAAA
GGGCGGTACCTGCAGATGAAGGCGAAGCGACAGGGCCACGCGGAGCCTCAGCCCTAG
Enzyme 2 GenBank Gene ID D88894 Link Image
Enzyme 2 GeneCard ID ACOT7 Link Image
Enzyme 2 GenAtlas ID ACOT7 Link Image
Enzyme 2 HGNC ID HGNC:24157 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p36.31-p36.11
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6336
Enzyme 3 Name Acyl-coenzyme A thioesterase 2
Enzyme 3 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 3 Gene Name ACOT2
Enzyme 3 Protein Sequence >Acyl-coenzyme A thioesterase 2
MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVP
ARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLG
ELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGR
LLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLL
AGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELC
LSMASFLKGITAAVVINGSVANVGGTLRYKGETLPPVGVNRNRIKVTKDGYADIVDVLNS
PLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPET
GHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGREGTIP
SKV
Enzyme 3 Number of Residues 483
Enzyme 3 Molecular Weight 53257
Enzyme 3 Theoretical pI 8.93
Enzyme 3 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 3 General Function Not Available
Enzyme 3 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 3 Pathways Not Available
Enzyme 3 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 887376 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P49753 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ACOT2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >937 bp
CCCCCGGGCTGCAGGAATTCCTGAATTCAAAATGGCCTCATCTCCTGCTGTCCTTCGAGC
GTCCCGGCTGTACCAATGGAGCCTGAAGAGTTCGGCGCAGTTCCTGGGGTCTCCACAGCT
GAGGCAGAACCTGGGCCCTTTCCTGGGATTGTGGACATGTTCGGGAACTGGAGGTGGCCT
GCTGGAGTATCGGGCTAGTCTGCTGGCTGGGAAGGGTTTTGCTGTGATGGCTCTGGCTTA
TTATAACTATGAAGACCTCCCCAAGACCATGGAGACGCTCCATCTGGAGTACTTTGAAGA
AGCCATGAACTACTTGCTCAGTCATCCCGAGGTAAAAGGTCCAGGAGTTGGGCTGCTTGG
AATTTCCAAAGGGGGTGAGCTCTGCCTTTCCATGGCCTCTTTCCTGAAGGGCATCACGGC
TGCTGTCGTCATCAACGGCTCTGTGGCCAATGTTGGGGGAACCTTACACTACAAGGGCGA
GACCCTGCCCCCTGTGGGCGTCAACAGAAATCGCATCAAGGTGACCAAAGATGGCTATGC
AGACATTGTGGATGTCCTGAACAGCCCTTTGGAAGGACCTGACCAGAAGAGCTTCATTCC
TGTGGAAAGGGCAGAGAGCACCTTCCTGTTCCTGGTAGGTCAGGATGACCACAACTGGAA
GAGTGAGTTCTATGCTAATGAGGCCTGTAAACGCTTGCAGGCCCATGGGAGGAGAAAGCC
CCAGATCATCTGTTACCCAGAGACAGGGCACTATATTGAGCCTCCTTACTTCCCCCTGTG
TCGGGCTTCCCTGCATGCCTTGGTGGGCAGTCCTATTATCTGGGGAGGGGAGCCCAGGGC
TCATGCCATGGCTCAGGTGGATGCTTGGAAACAACTCCAGACTTTCTTCCACAAACACTT
GGGTGGCCACGAGGGGACAATCCCATCAAAAGTGTAA
Enzyme 3 GenBank Gene ID L40401 Link Image
Enzyme 3 GeneCard ID ACOT2 Link Image
Enzyme 3 GenAtlas ID ACOT2 Link Image
Enzyme 3 HGNC ID HGNC:18431 Link Image
Enzyme 3 Chromosome Location 14
Enzyme 3 Locus 14q24.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6338
Enzyme 4 Name Acyl-coenzyme A thioesterase 8
Enzyme 4 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 4 Gene Name ACOT8
Enzyme 4 Protein Sequence >Acyl-coenzyme A thioesterase 8
MSSPQAPEDGQGCGDRGDPPGDLRSVLVTTVLNLEPLDEDLFRGRHYWVPAKRLFGGQIV
GQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSVKAVQHGKP
IFICQASFQQAQPSPMQHQFSMPTVPPPEELLDCETLIDQYLRDPNLQKRYPLALNRIAA
QEVPIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEGDMKMHCCVAAYISDYAFLGTAL
LPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAV
TCAQEGVIRVKPQVSESKL
Enzyme 4 Number of Residues 319
Enzyme 4 Molecular Weight 35915
Enzyme 4 Theoretical pI 7.60
Enzyme 4 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 4 General Function Lipid transport and metabolism
Enzyme 4 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 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 2318125 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O14734 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ACOT8_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >960 bp
ATGTCGTCCCCGCAGGCCCCAGAAGATGGGCAGGGCTGTGGCGACCGCGGCGATCCCCCT
GGGGACCTCCGTAGCGTCTTGGTCACGACCGTGCTCAACCTCGAGCCGCTGGACGAGGAT
CTCTTCAGAGGAAGGCATTACTGGGTACCGGCCAAGAGGCTGTTTGGTGGTCAGATCGTG
GGCCAGGCCCTGGTGGCTGCAGCCAAGTCTGTGAGTGAAGACGTCCACGTGCACTCCCTG
CACTGCTACTTTGTTCGGGCAGGGGACCCGAAGCTGCCAGTACTGTACCAAGTGGAGCGG
ACACGAACAGGGTCGAGCTTCTCGGTGCGCTCTGTGAAGGCCGTGCAACATGGGAAGCCC
ATCTTCATCTGCCAGGCCTCCTTCCAGCAGGCCCAGCCCAGCCCCATGCAGCACCAGTTC
TCCATGCCCACTGTGCCACCACCAGAAGAGCTGCTTGACTGTGAGACCCTCATTGACCAG
TATTTAAGGGACCCTAACCTCCAAAAGAGGTACCCATTGGCGCTCAACCGAATTGCTGCT
CAGGAGGTCCCCATTGAGATCAAGCCAGTAAACCCATCCCCCCTGAGCCAGCTGCAGAGA
ATGGAGCCCAAACAGATGTTCTGGGTGCGAGCCCGGGGCTATATTGGCGAGGGCGACATG
AAGATGCACTGCTGCGTGGCCGCCTATATCTCCGACTATGCCTTCTTGGGCACTGCACTG
CTGCCTCACCAGTGGCAGCACAAGGTGCACTTCATGGTCTCACTGGACCATTCCATGTGG
TTCCACGCCCCCTTCCGAGCTGACCACTGGATGCTCTATGAATGCGAGAGCCCCTGGGCC
GGTGGCTCTCGGGGGCTGGTCCATGGGCGGCTGTGGCGTCAGGATGGAGTCCTAGCTGTG
ACCTGTGCCCAGGAGGGCGTGATCCGAGTGAAGCCCCAGGTCTCAGAGAGCAAGCTGTAG
Enzyme 4 GenBank Gene ID AF014404 Link Image
Enzyme 4 GeneCard ID ACOT8 Link Image
Enzyme 4 GenAtlas ID ACOT8 Link Image
Enzyme 4 HGNC ID HGNC:15919 Link Image
Enzyme 4 Chromosome Location 20
Enzyme 4 Locus 20q13.12
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 8149
Enzyme 5 Name BC269730_2
Enzyme 5 Synonyms
  1. Hypothetical protein DKFZp762M2311
  2. Fatty acid desaturase 1
Enzyme 5 Gene Name DKFZp762M2311
Enzyme 5 Protein Sequence >BC269730_2
MAPDPVAAETAAQGPTPRYFTWDEVAQRSGCEERWLVIDRKVYNISEFTRRHPGGSRVIS
HYAGQDATDPFVAFHINKGLVKKYMNSLLIGELSPEQPSFEPTKNKELTDEFRELRATVE
RMGLMKANHVFFLLYLLHILLLDGAAWLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHD
FGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPFFFA
LGKILSVELGKQKKKYMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVIQRKKWVDLAWMI
TFYVRFFLTYVPLLGLKAFLGLFFIVRFLESNWFVWVTQMNHIPMHIDHDRNMDWVSTQL
QATCNVHKSAFNDWFSGHLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKHGIEYQSKPLL
SAFADIIHSLKESGQLWLDAYLHQ
Enzyme 5 Number of Residues 444
Enzyme 5 Molecular Weight 51965
Enzyme 5 Theoretical pI 9.15
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid biosynthesis
  • fatty acid desaturation
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
  • cell
  • membrane
Enzyme 5 General Function Lipid transport and metabolism
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 131-153
  • 266-288
  • 301-323
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID O60427 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name O60427_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AC004770 Link Image
Enzyme 5 GeneCard ID DKFZp762M2311 Link Image
Enzyme 5 GenAtlas ID DKFZp762M2311 Link Image
Enzyme 5 HGNC ID HGNC:3574 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Marquardt A, Stohr H, White K, Weber BH: cDNA cloning, genomic structure, and chromosomal localization of three members of the human fatty acid desaturase family. Genomics. 2000 Jun 1;66(2):175-83. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 15234
Enzyme 6 Name Acyl-CoA thioesterase 4
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name ACOT4
Enzyme 6 Protein Sequence >Acyl-CoA thioesterase 4
MSATLILEPPGRCCWNEPVRIAVRGLAPEQRVTLRASLRDEKGALFRAHARYCADACGEL
DLERAPALGGSFAGLEPMGLLWALEPEKPFWRFLKRDVQIPFVVELEVLDGHDPEPGRLL
CQAQHERHFLPPGVRRQSVRAGRVRATLFLPPGPGPFPGIIDIFGIGGGLLEYRASLLAG
HGFATLALAYYNFEDLPNNMDNISLEYFEEAVCYMLQHPQVKGPGIGLLGISLGADICLS
MASFLKNVSATVSINGSGISGNTAINYKHSSIPPLGYDLRRIKVAFSGLVDIVDIRNALV
GGYKNPSMIPIEKAQGPILLIVGQDDHNWRSELYAQTVSERLQAHGKEKPQIICYPGTGH
YIEPPYFPLCPASLHRLLNKHVIWGGEPRAHSKAQEDAWKQILAFFCKHLGGTQKTAVPK
L
Enzyme 6 Number of Residues 421
Enzyme 6 Molecular Weight 46274
Enzyme 6 Theoretical pI 7.95
Enzyme 6 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 6 General Function Not Available
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 60551129 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q5BKT6 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name Q5BKT6_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1266 bp
ATGTCAGCAACGCTGATCCTGGAGCCCCCAGGCCGCTGCTGCTGGAACGAGCCGGTGCGC
ATTGCCGTGCGCGGCCTGGCCCCGGAGCAGCGGGTTACGCTGCGCGCGTCCCTGCGCGAC
GAGAAGGGCGCGCTCTTCCGGGCCCACGCGCGCTACTGCGCCGACGCCTGCGGCGAGCTG
GACCTGGAGCGCGCACCCGCGCTGGGCGGCAGCTTCGCGGGACTCGAGCCCATGGGGCTG
CTCTGGGCCCTGGAACCCGAGAAGCCTTTTTGGCGCTTCCTGAAGCGGGACGTACAGATT
CCTTTTGTCGTGGAGTTGGAGGTGCTGGACGGCCACGACCCCGAGCCTGGACGGCTGCTG
TGCCAGGCGCAGCACGAGCGCCACTTCCTCCCGCCAGGGGTGCGGCGCCAGTCGGTGCGA
GCGGGCCGGGTGCGCGCCACGCTCTTCCTGCCGCCAGGACCTGGACCCTTCCCAGGGATC
ATTGACATCTTTGGTATTGGAGGGGGCCTCTTGGAATATCGAGCCAGCCTCCTTGCTGGC
CATGGCTTTGCCACGTTGGCTCTAGCTTATTATAACTTTGAAGATCTCCCCAATAACATG
GACAACATATCCCTGGAGTACTTCGAAGAAGCCGTATGCTACATGCTTCAACATCCCCAG
GTAAAAGGCCCAGGCATTGGGCTTTTGGGCATTTCTCTAGGAGCTGATATTTGTCTCTCA
ATGGCCTCATTCTTGAAGAATGTCTCAGCCACAGTTTCCATCAATGGATCTGGGATCAGT
GGGAACACAGCCATCAACTATAAGCACAGTAGCATTCCACCATTGGGCTATGACCTGAGG
AGAATCAAGGTAGCTTTCTCAGGCCTCGTGGACATCGTGGATATAAGGAATGCTCTCGTA
GGAGGGTACAAGAACCCCAGCATGATTCCAATAGAGAAGGCCCAGGGGCCCATCCTGCTC
ATTGTTGGTCAGGATGACCATAACTGGAGAAGTGAGTTGTATGCCCAAACAGTCTCTGAA
CGGTTACAGGCCCATGGAAAGGAAAAACCCCAGATCATCTGTTACCCTGGGACTGGGCAT
TACATCGAGCCTCCTTACTTCCCCCTGTGCCCAGCTTCCCTTCACAGATTACTGAACAAA
CATGTTATATGGGGTGGGGAGCCCAGGGCTCATTCTAAGGCCCAGGAAGATGCCTGGAAG
CAAATTCTAGCCTTCTTCTGCAAACACCTGGGAGGTACCCAGAAAACAGCTGTCCCTAAA
TTGTAA
Enzyme 6 GenBank Gene ID BC090945 Link Image
Enzyme 6 GeneCard ID Q5BKT6 Link Image
Enzyme 6 GenAtlas ID ACOT4 Link Image
Enzyme 6 HGNC ID HGNC:19748 Link Image
Enzyme 6 Chromosome Location 14
Enzyme 6 Locus 14q24.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available