| 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 |
- (5Z,8Z,11Z,14Z,17Z)-Eicosapentaenoate
- 5,8,11,14,17-Eicosapentaenoate
- 5,8,11,14,17-Eicosapentaenoic acid
- 5,8,11,14,17-Icosapentaenoate
- 5,8,11,14,17-Icosapentaenoic acid
- 5Z,8Z,11Z,14Z,17Z-Eicosapentaenoate
- 5Z,8Z,11Z,14Z,17Z-Eicosapentaenoic acid
- EPA
- Eicosapentaenoate
- Icosapent
- Icosapentaenoate
- Icosapentaenoic acid
- Icosapento
- Icosapentum
- Timnodonate
- Timnodonic acid
- all-cis-icosapentaenoate
- all-cis-icosapentaenoic acid
- cis-5,8,11,14,17-Eicosapentaenoate
- cis-5,8,11,14,17-Eicosapentaenoic acid
- (5Z,8Z,11Z,14Z,17Z)-Eicosapentaenoic acid
- Eicosapentaenoic acid
|
| Chemical IUPAC Name |
(5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoic acid |
| Chemical Formula |
C20H30O2 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
|
| Biofunction |
| — |
| Application |
| — |
| Source |
|
|
| 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  |
| BioCyc ID |
CPD-6941  |
| BiGG ID |
2218016  |
| Wikipedia Link |
Eicosapentaenoic acid  |
| NuGOwiki Link |
HMDB01999  |
| Metagene Link |
HMDB01999  |
| METLIN ID |
6423  |
| PubChem Compound |
446284  |
| PubChem Substance |
631225  |
| ChEBI ID |
28364  |
| 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 |
|
| 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
]
|
| 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
]
|
| 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
]
|
| 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
]
|
| 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
]
|
| 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
]
|
|
| 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
]
|
| 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
]
|
| 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
]
|
|
| 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
]
|
| 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
]
|
|
| OMIM ID |
|
| Pathways |
| Name |
SMPDB Link |
KEGG Link |
| Alpha Linolenic Acid and Linoleic Acid Metabolism |
SMP00018  |
map00592  |
|
| General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Wikipedia

|
| Metabolic Enzymes |
- Bile acid CoA:amino acid N-acyltransferase
- Cytosolic acyl coenzyme A thioester hydrolase
- Acyl-coenzyme A thioesterase 2
- Acyl-coenzyme A thioesterase 8
- BC269730_2
- Acyl-CoA thioesterase 4
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5821 |
| Enzyme 1 Name |
Bile acid CoA:amino acid N-acyltransferase |
| Enzyme 1 Synonyms |
- BAT
- BACAT
- Glycine N-choloyltransferase
- 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 |
- Bile Acid Biosynthesis (map00120
)
- Taurine and Hypotaurine Metabolism (map00430
)
|
| Enzyme 1 Reactions |
- palmitoyl-CoA + H2O = CoA + palmitate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
532505  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q14032  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
BAAT_HUMAN  |
| 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  |
| Enzyme 1 GeneCard ID |
BAAT  |
| Enzyme 1 GenAtlas ID |
BAAT  |
| Enzyme 1 HGNC ID |
HGNC:932  |
| Enzyme 1 Chromosome Location |
9 |
| Enzyme 1 Locus |
9q22.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
|
| 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 |
- Long chain acyl-CoA thioester hydrolase
- CTE-II
- CTE-IIa
- Brain acyl-CoA hydrolase
- 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 |
|
| 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 |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
2780414  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
O00154  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
BACH_HUMAN  |
| 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  |
| Enzyme 2 GeneCard ID |
ACOT7  |
| Enzyme 2 GenAtlas ID |
ACOT7  |
| Enzyme 2 HGNC ID |
HGNC:24157  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p36.31-p36.11 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6336 |
| Enzyme 3 Name |
Acyl-coenzyme A thioesterase 2 |
| Enzyme 3 Synonyms |
- Acyl-CoA thioesterase 2
- Peroxisomal acyl-coenzyme A thioester hydrolase 2a
- Peroxisomal long-chain acyl-coA thioesterase 2
- ZAP128
- 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 |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
887376  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P49753  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
ACOT2_HUMAN  |
| 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  |
| Enzyme 3 GeneCard ID |
ACOT2  |
| Enzyme 3 GenAtlas ID |
ACOT2  |
| Enzyme 3 HGNC ID |
HGNC:18431  |
| Enzyme 3 Chromosome Location |
14 |
| Enzyme 3 Locus |
14q24.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6338 |
| Enzyme 4 Name |
Acyl-coenzyme A thioesterase 8 |
| Enzyme 4 Synonyms |
- Choloyl-coenzyme A thioesterase
- Acyl-CoA thioesterase 8
- Peroxisomal acyl-coenzyme A thioester hydrolase 1
- PTE-1
- Peroxisomal long-chain acyl-coA thioesterase 1
- HIV-Nef-associated acyl coA thioesterase
- Thioesterase II
- hTE
- hACTEIII
- hACTE-III
- 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 |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
2318125  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
O14734  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
ACOT8_HUMAN  |
| 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  |
| Enzyme 4 GeneCard ID |
ACOT8  |
| Enzyme 4 GenAtlas ID |
ACOT8  |
| Enzyme 4 HGNC ID |
HGNC:15919  |
| Enzyme 4 Chromosome Location |
20 |
| Enzyme 4 Locus |
20q13.12 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
8149 |
| Enzyme 5 Name |
BC269730_2 |
| Enzyme 5 Synonyms |
- Hypothetical protein DKFZp762M2311
- 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 |
|
|
| 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 |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
Not Available |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
O60427  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
O60427_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
Not Available |
| Enzyme 5 GenBank Gene ID |
AC004770  |
| Enzyme 5 GeneCard ID |
DKFZp762M2311  |
| Enzyme 5 GenAtlas ID |
DKFZp762M2311  |
| Enzyme 5 HGNC ID |
HGNC:3574  |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- 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
]
|
| 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 |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
60551129  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q5BKT6  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
Q5BKT6_HUMAN  |
| 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  |
| Enzyme 6 GeneCard ID |
Q5BKT6  |
| Enzyme 6 GenAtlas ID |
ACOT4  |
| Enzyme 6 HGNC ID |
HGNC:19748  |
| Enzyme 6 Chromosome Location |
14 |
| Enzyme 6 Locus |
14q24.3 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- 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
]
|
| Enzyme 6 Metabolite References |
Not Available |