Human Metabolome Database Version 2.5

Showing metabocard for 8,11,14-Eicosatrienoic acid (HMDB02925)

Legend: metabolite field enzyme field

Version

2.5

Creation Date

2006-05-22 16:12:20

Update Date

2010-04-21 19:57:04

Accession Number

HMDB02925

Secondary Accession Numbers

HMDB06735

Common Name

8,11,14-Eicosatrienoic acid

Description

8,11,14-Eicosatrienoic acid is a 20-carbon-chain omega-6 fatty acid, unsaturated at positions 8, 11, and 14. It differs from arachidonic acid (5,8,11,14-eicosatetraenoic acid) only at position 5. 8,11,14-Eicosatrienoic acid is also known as Dihomo-gamma-linolenic acid (DGLA). In physiological literature, it is given the name 20:3(n-6). DGLA is the elongation product of the 18 carbon gamma-linolenic acid (GLA). DGLA can be converted into prostaglandin E1 (PGE1). PGE1 inhibits platelet aggregation and also exerts a vasodilatory effect. DGLA competes with arachadonic acid for COX and lipoxygenase, inhibiting the production of arachadonic acid's eicosanoids

Synonyms

(8Z,11Z,14Z)-Icosatrienoate
(8Z,11Z,14Z)-Icosatrienoic acid
(Z,Z,Z)-8,11,14-Eicosatrienoate
(Z,Z,Z)-8,11,14-Eicosatrienoic acid
(Z,Z,Z)-8,11,14-Icosatrienoate
(Z,Z,Z)-8,11,14-Icosatrienoic acid
(Z,Z,Z)-icosatri-8,11,14-enoate
(Z,Z,Z)-icosatri-8,11,14-enoic acid
8,11,14-Eicosatrienoate
8,11,14-Eicosatrienoic acid
8,11,14-Icosatrienoate
8,11,14-all-cis-Eicosatrienoate
8,11,14-all-cis-Eicosatrienoic acid
8Z,11Z,14Z-eicosatrienoate
8Z,11Z,14Z-eicosatrienoic acid
Bishomo-gamma-linolenate
Bishomo-gamma-linolenic acid
DGLA
Dihomo-gamma-linolenate
Dihomo-gamma-linolenic acid
Eicosatrienoate
Homo-gamma-linolenate
all-cis-8,11,14-Eicosatrienoate
all-cis-8,11,14-Eicosatrienoic acid
cis,cis,cis-8,11,14-Eicosatrienoate
cis,cis,cis-8,11,14-Eicosatrienoic acid
cis-8,11,14-Eicosatrienoate
cis-8,11,14-Eicosatrienoic acid
cis-8,cis-11,cis-14-Eicosatrienoate
cis-8,cis-11,cis-14-Eicosatrienoic acid
gamma-Homolinolenate
gamma-Homolinolenic acid
8,11,14-Icosatrienoic acid
Eicosatrienoic acid

Chemical IUPAC Name

(8E,11E,14E)-icosa-8,11,14-trienoic acid

Chemical Formula

C₂₀H₃₄O₂

Chemical 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

306.483

Monoisotopic Molecular Weight

306.255890

Isomeric SMILES

CCCCCC=C/CC=C/CC=C/CCCCCCC(O)=O

Canonical SMILES

CCCCCC=CCC=CCC=CCCCCCCC(O)=O

KEGG Compound ID

BioCyc ID

BiGG ID

Wikipedia Link

NuGOwiki Link

Metagene Link

METLIN ID

PubChem Compound

PubChem Substance

ChEBI ID

Not Available

CAS Registry Number

1783-84-2

InChI Identifier

InChI=1/C20H34O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-18-19-20(21)22/h6-7,9-10,12-13H,2-5,8,11,14-19H2,1H3,(H,21,22)/b7-6-,10-9-,13-12-

Synthesis Reference

Not Available

Melting Point (Experimental)

Not Available

Experimental Water Solubility

Not Available Source: PhysProp

Predicted Water Solubility

7.71e-05 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS

Physiological Charge

-1

State

Solid

Experimental LogP/Hydrophobicity

Not Available Source: PhysProp

Predicted LogP/Hydrophobicity

7.24 [Predicted by ALOGPS]; 6.777 [Predicted by PubChem via XLOGP] Calculated using ALOGPS

Material Safety Data Sheet (MSDS)

Show PDF/HTML

MOL File

Show

SDF File

Show

PDB File

Show

2D Structure

3D Structure

Experimental PDB ID

Not Available

Experimental ¹H NMR Spectrum

Download Spectrum
Download FID (Bruker)
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
Medium Energy
Download File Show Experimental Conditions
High Energy
Download File Show Experimental Conditions

Simplified TOCSY Spectrum

Not Available

BMRB Spectrum

Not Available

Cellular Location

Membrane (Predicted from LogP)
Cytoplasm
Extracellular

Biofluid Location

Blood

Tissue Location

Tissue	References
Adipose Tissue	—
Epidermis	—

Concentrations (Normal)

Biofluid	Blood
Value	0.420 +/- 0.207 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 ]

Concentrations (Abnormal)

Not Available

Associated Disorders

Not Available

OMIM ID

Not Available

Pathways

Name	SMPDB Link	KEGG Link
Alpha Linolenic Acid and Linoleic Acid Metabolism	SMP00018	map00592

General References

Abraham RD, Riemersma RA, Elton RA, Macintyre C, Oliver MF: Effects of safflower oil and evening primrose oil in men with a low dihomo-gamma-linolenic level. Atherosclerosis. 1990 Apr;81(3):199-208. [PubMed ]
Du L, Yermalitsky V, Hachey DL, Jagadeesh SG, Falck JR, Keeney DS: A biosynthetic pathway generating 12-hydroxy-5,8,14-eicosatrienoic acid from arachidonic acid is active in mouse skin microsomes. J Pharmacol Exp Ther. 2006 Jan;316(1):371-9. Epub 2005 Sep 16. [PubMed ]
Hamilton RM, Gillespie CT, Cook HW: Relationships between levels of essential fatty acids and zinc in plasma of cystic fibrosis patients. Lipids. 1981 May;16(5):374-6. [PubMed ]
Thijs C, Houwelingen A, Poorterman I, Mordant A, van den Brandt P: Essential fatty acids in breast milk of atopic mothers: comparison with non-atopic mothers, and effect of borage oil supplementation. Eur J Clin Nutr. 2000 Mar;54(3):234-8. [PubMed ]
Emken EA, Adlof RO, Duval SM, Nelson GJ: Influence of dietary arachidonic acid on metabolism in vivo of 8cis,11cis,14-eicosatrienoic acid in humans. Lipids. 1997 Apr;32(4):441-8. [PubMed ]
Melnik BC, Plewig G: Is the origin of atopy linked to deficient conversion of omega-6-fatty acids to prostaglandin E1? J Am Acad Dermatol. 1989 Sep;21(3 Pt 1):557-63. [PubMed ]
Wikipedia

Metabolic Enzymes

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

BAAT_C (PF08840 )
Bile_Hydr_Trans (PF04775 )

Enzyme 1 Signals

None

Enzyme 1 Transmembrane Regions

None

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 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

Enzyme 1 GeneCard ID

Enzyme 1 GenAtlas ID

Enzyme 1 HGNC ID

Enzyme 1 Chromosome Location

Enzyme 1 Locus

9q22.3

Enzyme 1 SNPs

SNPJam Report Link Image

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
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

4HBT (PF03061 )

Enzyme 2 Signals

1-19

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 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

Enzyme 2 GeneCard ID

ACOT7

Enzyme 2 GenAtlas ID

ACOT7

Enzyme 2 HGNC ID

HGNC:24157 Link Image

Enzyme 2 Chromosome Location

Enzyme 2 Locus

1p36.31-p36.11

Enzyme 2 SNPs

SNPJam Report Link Image

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

Enzyme 3 Pathways

Not Available

Enzyme 3 Reactions

palmitoyl-CoA + H2O = CoA + palmitate

Enzyme 3 Pfam Domain Function

BAAT_C (PF08840 )
Bile_Hydr_Trans (PF04775 )

Enzyme 3 Signals

None

Enzyme 3 Transmembrane Regions

None

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 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

Enzyme 3 GeneCard ID

ACOT2

Enzyme 3 GenAtlas ID

ACOT2

Enzyme 3 HGNC ID

HGNC:18431 Link Image

Enzyme 3 Chromosome Location

Enzyme 3 Locus

14q24.3

Enzyme 3 SNPs

SNPJam Report Link Image

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

Acyl_CoA_thio (PF02551 )

Enzyme 4 Signals

None

Enzyme 4 Transmembrane Regions

None

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 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

Enzyme 4 GeneCard ID

ACOT8

Enzyme 4 GenAtlas ID

ACOT8

Enzyme 4 HGNC ID

HGNC:15919 Link Image

Enzyme 4 Chromosome Location

Enzyme 4 Locus

20q13.12

Enzyme 4 SNPs

SNPJam Report Link Image

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

15234

Enzyme 5 Name

Acyl-CoA thioesterase 4

Enzyme 5 Synonyms

Not Available

Enzyme 5 Gene Name

ACOT4

Enzyme 5 Protein Sequence

>Acyl-CoA thioesterase 4

MSATLILEPPGRCCWNEPVRIAVRGLAPEQRVTLRASLRDEKGALFRAHARYCADACGEL
DLERAPALGGSFAGLEPMGLLWALEPEKPFWRFLKRDVQIPFVVELEVLDGHDPEPGRLL
CQAQHERHFLPPGVRRQSVRAGRVRATLFLPPGPGPFPGIIDIFGIGGGLLEYRASLLAG
HGFATLALAYYNFEDLPNNMDNISLEYFEEAVCYMLQHPQVKGPGIGLLGISLGADICLS
MASFLKNVSATVSINGSGISGNTAINYKHSSIPPLGYDLRRIKVAFSGLVDIVDIRNALV
GGYKNPSMIPIEKAQGPILLIVGQDDHNWRSELYAQTVSERLQAHGKEKPQIICYPGTGH
YIEPPYFPLCPASLHRLLNKHVIWGGEPRAHSKAQEDAWKQILAFFCKHLGGTQKTAVPK
L

Enzyme 5 Number of Residues

421

Enzyme 5 Molecular Weight

46274

Enzyme 5 Theoretical pI

7.95

Enzyme 5 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 5 General Function

Not Available

Enzyme 5 Specific Function

Not Available

Enzyme 5 Pathways

Not Available

Enzyme 5 Reactions

Not Available

Enzyme 5 Pfam Domain Function

BAAT_C (PF08840 )
Bile_Hydr_Trans (PF04775 )

Enzyme 5 Signals

None

Enzyme 5 Transmembrane Regions

None

Enzyme 5 Essentiality

Not Available

Enzyme 5 GenBank ID Protein

60551129

Enzyme 5 UniProtKB/Swiss-Prot ID

Q5BKT6

Enzyme 5 UniProtKB/Swiss-Prot Entry Name

Q5BKT6_HUMAN Link Image

Enzyme 5 PDB ID

Not Available

Enzyme 5 Cellular Location

Not Available

Enzyme 5 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 5 GenBank Gene ID

BC090945

Enzyme 5 GeneCard ID

Q5BKT6

Enzyme 5 GenAtlas ID

ACOT4

Enzyme 5 HGNC ID

HGNC:19748 Link Image

Enzyme 5 Chromosome Location

Enzyme 5 Locus

14q24.3

Enzyme 5 SNPs

SNPJam Report Link Image

Enzyme 5 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 5 Metabolite References

Not Available

We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

Showing metabocard for 8,11,14-Eicosatrienoic acid (HMDB02925)