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Acyl-coenzyme A thioesterase 8 (Acyl-CoA thioesterase 8) (EC 3.1.2.27) (Choloyl-coenzyme A thioesterase) (HIV-Nef-associated acyl-CoA thioesterase) (PTE-2) (Peroxisomal acyl-coenzyme A thioester hydrolase 1) (PTE-1) (Peroxisomal long-chain acyl-CoA thioesterase 1) (Thioesterase II) (hACTE-III) (hACTEIII) (hTE)

 ACOT8_HUMAN             Reviewed;         319 AA.
O14734; O15261; Q17RX4;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
03-JUL-2019, entry version 177.
RecName: Full=Acyl-coenzyme A thioesterase 8;
Short=Acyl-CoA thioesterase 8;
EC=3.1.2.1 {ECO:0000269|PubMed:10944470, ECO:0000269|PubMed:9299485};
EC=3.1.2.11 {ECO:0000250|UniProtKB:P58137};
EC=3.1.2.2 {ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485};
EC=3.1.2.3 {ECO:0000250|UniProtKB:P58137};
EC=3.1.2.5 {ECO:0000250|UniProtKB:P58137};
AltName: Full=Choloyl-coenzyme A thioesterase;
EC=3.1.2.27 {ECO:0000269|PubMed:9299485};
AltName: Full=HIV-Nef-associated acyl-CoA thioesterase;
AltName: Full=Peroxisomal acyl-CoA thioesterase 2 {ECO:0000303|PubMed:11755680};
Short=PTE-2 {ECO:0000303|PubMed:11755680};
AltName: Full=Peroxisomal acyl-coenzyme A thioester hydrolase 1;
Short=PTE-1;
AltName: Full=Peroxisomal long-chain acyl-CoA thioesterase 1;
AltName: Full=Thioesterase II;
Short=hACTE-III;
Short=hACTEIII;
Short=hTE;
Name=ACOT8; Synonyms=ACTEIII, PTE1 {ECO:0000303|PubMed:10092594};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION), AND TISSUE
SPECIFICITY.
PubMed=9299485; DOI=10.1006/bbrc.1997.7217;
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. 238:234-239(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH
HIV-1 NEF (MICROBIAL INFECTION), AND TISSUE SPECIFICITY.
TISSUE=Lymphoid tissue;
PubMed=9153233; DOI=10.1074/jbc.272.21.13779;
Liu L.X., 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. 272:13779-13785(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
TISSUE=Muscle;
PubMed=10092594; DOI=10.1074/jbc.274.14.9216;
Jones J.M., Nau K., Geraghty M.T., Erdmann R., Gould S.J.;
"Identification of peroxisomal acyl-CoA thioesterases in yeast and
humans.";
J. Biol. Chem. 274:9216-9223(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=10944470; DOI=10.1006/bbrc.2000.3285;
Jones J.M., Gould S.J.;
"Identification of PTE2, a human peroxisomal long-chain acyl-CoA
thioesterase.";
Biochem. Biophys. Res. Commun. 275:233-240(2000).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-78.
PubMed=15194431; DOI=10.1016/j.yexcr.2004.02.029;
Ishizuka M., Toyama Y., Watanabe H., Fujiki Y., Takeuchi A.,
Yamasaki S., Yuasa S., Miyazaki M., Nakajima N., Taki S., Saito T.;
"Overexpression of human acyl-CoA thioesterase upregulates peroxisome
biogenesis.";
Exp. Cell Res. 297:127-141(2004).
[8]
REVIEW.
PubMed=11755680; DOI=10.1016/S0163-7827(01)00017-0;
Hunt M.C., Alexson S.E.H.;
"The role Acyl-CoA thioesterases play in mediating intracellular lipid
metabolism.";
Prog. Lipid Res. 41:99-130(2002).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Acyl-coenzyme A (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 (PubMed:9299485, PubMed:9153233, PubMed:15194431). Acyl-
coenzyme A thioesterase 8/ACOT8 display no strong substrate
specificity with respect to the carboxylic acid moiety of Acyl-
CoAs (By similarity). Hydrolyzes medium length (C2 to C20)
straight-chain, saturated and unsaturated acyl-CoAS but is
inactive towards substrates with longer aliphatic chains
(PubMed:9299485, PubMed:9153233). Moreover, it catalyzes the
hydrolysis of CoA esters of bile acids, such as choloyl-CoA and
chenodeoxycholoyl-CoA and competes with bile acid CoA:amino acid
N-acyltransferase (BAAT) (By similarity). ACOT8 is also able to
hydrolyze CoA esters of dicarboxylic acids (By similarity). It is
involved in the metabolic regulation of peroxisome proliferation
(PubMed:15194431). {ECO:0000250|UniProtKB:P58137,
ECO:0000269|PubMed:15194431, ECO:0000269|PubMed:9153233,
ECO:0000269|PubMed:9299485}.
-!- FUNCTION: (Microbial infection) May mediate Nef-induced down-
regulation of CD4 cell-surface expression (PubMed:9153233).
{ECO:0000269|PubMed:9153233}.
-!- CATALYTIC ACTIVITY:
Reaction=choloyl-CoA + H2O = cholate + CoA + H(+);
Xref=Rhea:RHEA:14541, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29747, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373;
EC=3.1.2.27; Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14542;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=chenodeoxycholoyl-CoA + H2O = chenodeoxycholate + CoA +
H(+); Xref=Rhea:RHEA:31511, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:36234, ChEBI:CHEBI:57287,
ChEBI:CHEBI:62989; EC=3.1.2.27;
Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31512;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + H2O = acetate + CoA + H(+);
Xref=Rhea:RHEA:20289, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30089, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288;
EC=3.1.2.1; Evidence={ECO:0000269|PubMed:10944470,
ECO:0000269|PubMed:9299485};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290;
Evidence={ECO:0000305|PubMed:9299485};
-!- CATALYTIC ACTIVITY:
Reaction=butanoyl-CoA + H2O = butanoate + CoA + H(+);
Xref=Rhea:RHEA:40111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:17968, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371;
Evidence={ECO:0000269|PubMed:10944470,
ECO:0000269|PubMed:9299485};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
Evidence={ECO:0000305|PubMed:9299485};
-!- CATALYTIC ACTIVITY:
Reaction=2-methylpropanoyl-CoA + H2O = 2-methylpropanoate + CoA +
H(+); Xref=Rhea:RHEA:40799, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:48944, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57338; Evidence={ECO:0000269|PubMed:10944470};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40800;
Evidence={ECO:0000305|PubMed:10944470};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate;
Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620;
Evidence={ECO:0000269|PubMed:9153233};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116;
Evidence={ECO:0000305|PubMed:9153233};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate;
Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386;
Evidence={ECO:0000269|PubMed:10944470,
ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
Evidence={ECO:0000305|PubMed:9299485};
-!- CATALYTIC ACTIVITY:
Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+);
Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
Evidence={ECO:0000269|PubMed:10944470,
ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
Evidence={ECO:0000305|PubMed:9299485};
-!- CATALYTIC ACTIVITY:
Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
Evidence={ECO:0000269|PubMed:9153233};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
Evidence={ECO:0000305|PubMed:9153233};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
Evidence={ECO:0000269|PubMed:10944470,
ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
Evidence={ECO:0000305|PubMed:9299485};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379;
EC=3.1.2.2; Evidence={ECO:0000269|PubMed:9153233,
ECO:0000269|PubMed:9299485};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
Evidence={ECO:0000305|PubMed:9299485};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
Evidence={ECO:0000269|PubMed:9299485};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
Evidence={ECO:0000305|PubMed:9299485};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + malonyl-CoA = CoA + H(+) + malonate;
Xref=Rhea:RHEA:40219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15792, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384;
Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40220;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=acetoacetyl-CoA + H2O = acetoacetate + CoA + H(+);
Xref=Rhea:RHEA:15673, ChEBI:CHEBI:13705, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287;
EC=3.1.2.11; Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15674;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + propanoyl-CoA = CoA + H(+) + propanoate;
Xref=Rhea:RHEA:40103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:17272, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392;
Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40104;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + succinyl-CoA = CoA + H(+) + succinate;
Xref=Rhea:RHEA:11516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30031, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292;
EC=3.1.2.3; Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11517;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=glutaryl-CoA + H2O = CoA + glutarate + H(+);
Xref=Rhea:RHEA:40575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30921, ChEBI:CHEBI:57287, ChEBI:CHEBI:57378;
Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40576;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + hexanedioyl-CoA = CoA + H(+) + hexanedioate;
Xref=Rhea:RHEA:40583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:17128, ChEBI:CHEBI:57287, ChEBI:CHEBI:76327;
Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40584;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + octanedioyl-CoA = CoA + H(+) + octanedioate;
Xref=Rhea:RHEA:40587, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57287, ChEBI:CHEBI:76282, ChEBI:CHEBI:76317;
Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40588;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=decanedioyl-CoA + H2O = CoA + decanedioate + H(+);
Xref=Rhea:RHEA:40591, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57287, ChEBI:CHEBI:76283, ChEBI:CHEBI:76316;
Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40592;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=dodecanedioyl-CoA + H2O = CoA + dodecanedioate + H(+);
Xref=Rhea:RHEA:40595, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57287, ChEBI:CHEBI:76273, ChEBI:CHEBI:76315;
Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40596;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=(9Z)-tetradecenoyl-CoA + H2O = (9Z)-tetradecenoate + CoA
+ H(+); Xref=Rhea:RHEA:40135, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:32370, ChEBI:CHEBI:57287,
ChEBI:CHEBI:65060; Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40136;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA +
H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287,
ChEBI:CHEBI:61540; Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA +
H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-
octadecadienoate + CoA + H(+); Xref=Rhea:RHEA:40143,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
ChEBI:CHEBI:57287, ChEBI:CHEBI:57383;
Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+);
Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380;
Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O =
(5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA + H(+);
Xref=Rhea:RHEA:40151, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:32395, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368;
Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=4,8-dimethylnonanoyl-CoA + H2O = 4,8-dimethylnonanoate +
CoA + H(+); Xref=Rhea:RHEA:40223, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061,
ChEBI:CHEBI:77063; Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40224;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=2,6-dimethylheptanoyl-CoA + H2O = 2,6-dimethylheptanoate
+ CoA + H(+); Xref=Rhea:RHEA:59952, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:84847,
ChEBI:CHEBI:143533; Evidence={ECO:0000250|UniProtKB:Q8VHK0};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59953;
Evidence={ECO:0000250|UniProtKB:Q8VHK0};
-!- CATALYTIC ACTIVITY:
Reaction=(3S)-hydroxy-3-methylglutaryl-CoA + H2O = 3-hydroxy-3-
methylglutarate + CoA + H(+); Xref=Rhea:RHEA:16305,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17325,
ChEBI:CHEBI:43074, ChEBI:CHEBI:57287; EC=3.1.2.5;
Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16306;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-
CoA + H2O = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-
oate + CoA + H(+); Xref=Rhea:RHEA:59936, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:63001,
ChEBI:CHEBI:85674; Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59937;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=2-methyloctadecanoyl-CoA + H2O = 2-methyloctadecanoate +
CoA + H(+); Xref=Rhea:RHEA:59940, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:143530,
ChEBI:CHEBI:143531; Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59941;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + prostaglandin F2alpha-CoA = CoA + H(+) +
prostaglandin F2alpha; Xref=Rhea:RHEA:59948, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57404,
ChEBI:CHEBI:143532; Evidence={ECO:0000250|UniProtKB:P58137};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59949;
Evidence={ECO:0000250|UniProtKB:P58137};
-!- ACTIVITY REGULATION: Inhibited by CoASH (IC(50)=10-15 uM). Also
inhibited by cysteine-reactive agents.
{ECO:0000250|UniProtKB:P58137}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=10.1 uM for decanoyl-CoA {ECO:0000269|PubMed:9153233};
Vmax=7.1 umol/min/mg enzyme {ECO:0000269|PubMed:9153233};
-!- PATHWAY: Lipid metabolism; fatty acid metabolism.
{ECO:0000305|PubMed:10944470, ECO:0000305|PubMed:9299485}.
-!- SUBUNIT: Homodimer (By similarity).
{ECO:0000250|UniProtKB:P58137}.
-!- SUBUNIT: (Microbial infection) Interacts with human
immunodeficiency virus (HIV-1) Nef (via middle region); this
interaction enhances ACOT8 Acyl-CoA thioesterase activity and
occurs in a Nef myristoylation-independent manner
(PubMed:9299485). According to a second report, the interaction
with HIV-1 Nef occurs in a Nef myristoylation-independent manner
but does not enhance ACOT8 Acyl-CoA thioesterase activity
(PubMed:9153233). {ECO:0000269|PubMed:9153233,
ECO:0000269|PubMed:9299485}.
-!- INTERACTION:
P04601:nef (xeno); NbExp=7; IntAct=EBI-1237371, EBI-6164028;
P50542:PEX5; NbExp=3; IntAct=EBI-1237371, EBI-597835;
Q04864:REL; NbExp=3; IntAct=EBI-1237371, EBI-307352;
-!- SUBCELLULAR LOCATION: Peroxisome matrix
{ECO:0000269|PubMed:10092594, ECO:0000269|PubMed:15194431}.
Note=Predominantly localized in the peroxisome but a localization
to the cytosol cannot be excluded. {ECO:0000269|PubMed:10092594,
ECO:0000269|PubMed:15194431}.
-!- TISSUE SPECIFICITY: Detected in a T-cell line (at protein level).
Ubiquitous (PubMed:9153233, PubMed:9299485).
{ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485}.
-!- INDUCTION: Regulated by peroxisome proliferator (such as
Clofibrate), via the peroxisome proliferator-activated receptors
(PPARs). {ECO:0000250}.
-!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF014404; AAB71665.1; -; mRNA.
EMBL; X86032; CAA60024.1; -; mRNA.
EMBL; AF124264; AAD27616.1; -; mRNA.
EMBL; AL008726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC117155; AAI17156.1; -; mRNA.
EMBL; BC117157; AAI17158.1; -; mRNA.
CCDS; CCDS13378.1; -.
PIR; JC5644; JC5644.
RefSeq; NP_005460.2; NM_005469.3.
SMR; O14734; -.
BioGrid; 115323; 19.
DIP; DIP-38179N; -.
IntAct; O14734; 13.
STRING; 9606.ENSP00000217455; -.
SwissLipids; SLP:000000591; -.
iPTMnet; O14734; -.
PhosphoSitePlus; O14734; -.
SwissPalm; O14734; -.
BioMuta; ACOT8; -.
EPD; O14734; -.
jPOST; O14734; -.
MaxQB; O14734; -.
PaxDb; O14734; -.
PeptideAtlas; O14734; -.
PRIDE; O14734; -.
ProteomicsDB; 48196; -.
DNASU; 10005; -.
Ensembl; ENST00000217455; ENSP00000217455; ENSG00000101473.
GeneID; 10005; -.
KEGG; hsa:10005; -.
UCSC; uc002xqa.3; human.
CTD; 10005; -.
DisGeNET; 10005; -.
GeneCards; ACOT8; -.
HGNC; HGNC:15919; ACOT8.
HPA; CAB010261; -.
MIM; 608123; gene.
neXtProt; NX_O14734; -.
OpenTargets; ENSG00000101473; -.
PharmGKB; PA33941; -.
eggNOG; KOG3016; Eukaryota.
eggNOG; COG1946; LUCA.
GeneTree; ENSGT00390000004207; -.
HOGENOM; HOG000246495; -.
InParanoid; O14734; -.
KO; K11992; -.
OMA; WLLYAMD; -.
OrthoDB; 826588at2759; -.
PhylomeDB; O14734; -.
TreeFam; TF315124; -.
BRENDA; 3.1.2.2; 2681.
BRENDA; 3.1.2.20; 2681.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-HSA-389887; Beta-oxidation of pristanoyl-CoA.
Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
Reactome; R-HSA-9033241; Peroxisomal protein import.
UniPathway; UPA00199; -.
ChiTaRS; ACOT8; human.
GeneWiki; ACOT8; -.
GenomeRNAi; 10005; -.
PRO; PR:O14734; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101473; Expressed in 194 organ(s), highest expression level in mucosa of transverse colon.
ExpressionAtlas; O14734; baseline and differential.
Genevisible; O14734; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
GO; GO:0047603; F:acetoacetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0003986; F:acetyl-CoA hydrolase activity; TAS:Reactome.
GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0033882; F:choloyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016289; F:CoA hydrolase activity; TAS:Reactome.
GO; GO:0047994; F:hydroxymethylglutaryl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0052815; F:medium-chain acyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0004778; F:succinyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0006637; P:acyl-CoA metabolic process; IDA:UniProtKB.
GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
GO; GO:0043649; P:dicarboxylic acid catabolic process; IDA:UniProtKB.
GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
GO; GO:0009062; P:fatty acid catabolic process; IBA:GO_Central.
GO; GO:0045225; P:negative regulation of CD4 biosynthetic process; IDA:UniProtKB.
GO; GO:0016559; P:peroxisome fission; IDA:UniProtKB.
GO; GO:0006625; P:protein targeting to peroxisome; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.10.129.90; -; 1.
InterPro; IPR042171; Acyl-CoA_hotdog.
InterPro; IPR003703; Acyl_CoA_thio.
InterPro; IPR029069; HotDog_dom_sf.
PANTHER; PTHR11066; PTHR11066; 1.
SUPFAM; SSF54637; SSF54637; 2.
TIGRFAMs; TIGR00189; tesB; 1.
1: Evidence at protein level;
Complete proteome; Fatty acid metabolism; Host-virus interaction;
Hydrolase; Lipid metabolism; Peroxisome; Peroxisome biogenesis;
Reference proteome; Serine esterase.
CHAIN 1 319 Acyl-coenzyme A thioesterase 8.
/FTId=PRO_0000202152.
MOTIF 317 319 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 232 232 Charge relay system. {ECO:0000250}.
ACT_SITE 254 254 Charge relay system. {ECO:0000250}.
ACT_SITE 304 304 Charge relay system. {ECO:0000250}.
MUTAGEN 78 78 H->A: Reduces Acyl-CoA thioesterase
activity and peroxisome proliferation.
{ECO:0000269|PubMed:15194431}.
CONFLICT 291 293 LWR -> VWS (in Ref. 2; CAA60024).
{ECO:0000305}.
CONFLICT 319 319 L -> R (in Ref. 2; CAA60024).
{ECO:0000305}.
SEQUENCE 319 AA; 35914 MW; 8345C6E5EABF3326 CRC64;
MSSPQAPEDG QGCGDRGDPP GDLRSVLVTT VLNLEPLDED LFRGRHYWVP AKRLFGGQIV
GQALVAAAKS VSEDVHVHSL HCYFVRAGDP KLPVLYQVER TRTGSSFSVR SVKAVQHGKP
IFICQASFQQ AQPSPMQHQF SMPTVPPPEE LLDCETLIDQ YLRDPNLQKR YPLALNRIAA
QEVPIEIKPV NPSPLSQLQR MEPKQMFWVR ARGYIGEGDM KMHCCVAAYI SDYAFLGTAL
LPHQWQHKVH FMVSLDHSMW FHAPFRADHW MLYECESPWA GGSRGLVHGR LWRQDGVLAV
TCAQEGVIRV KPQVSESKL


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WP1116: Arachidonate Epoxygenase Epoxide Hydrolase
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Related Genes :
[Acot8 Pte1] Acyl-coenzyme A thioesterase 8 (Acyl-CoA thioesterase 8) (EC 3.1.2.1) (EC 3.1.2.11) (EC 3.1.2.2) (EC 3.1.2.3) (EC 3.1.2.5) (Choloyl-coenzyme A thioesterase) (EC 3.1.2.27) (Peroxisomal acyl-CoA thioesterase 2) (PTE-2) (Peroxisomal acyl-coenzyme A thioester hydrolase 1) (PTE-1) (Peroxisomal long-chain acyl-CoA thioesterase 1)
[Acot3 Pte1a Pte2 Pte2a] Acyl-coenzyme A thioesterase 3 (Acyl-CoA thioesterase 3) (EC 3.1.2.2) (PTE-Ia) (Peroxisomal acyl-coenzyme A thioester hydrolase 2a) (Peroxisomal long-chain acyl-CoA thioesterase 2)
[Acot4 Pte1b Pte2b] Peroxisomal succinyl-coenzyme A thioesterase (EC 3.1.2.3) (Acyl-coenzyme A thioesterase 4) (Acyl-CoA thioesterase 4) (PTE-2b) (Peroxisomal acyl coenzyme A thioester hydrolase Ib) (Peroxisomal long-chain acyl-CoA thioesterase Ib) (PTE-Ib)
[Acot1 Cte1] Acyl-coenzyme A thioesterase 1 (Acyl-CoA thioesterase 1) (EC 3.1.2.-) (CTE-I) (Inducible cytosolic acyl-coenzyme A thioester hydrolase) (LACH2) (ACH2) (Long chain acyl-CoA thioester hydrolase) (Long chain acyl-CoA hydrolase) (Palmitoyl-coenzyme A thioesterase) (EC 3.1.2.2)
[Acot1 Cte1] Acyl-coenzyme A thioesterase 1 (Acyl-CoA thioesterase 1) (EC 3.1.2.-) (CTE-I) (Inducible cytosolic acyl-coenzyme A thioester hydrolase) (Long chain acyl-CoA thioester hydrolase) (Long chain acyl-CoA hydrolase) (Palmitoyl-coenzyme A thioesterase) (EC 3.1.2.2)
[Acot2 Mte1] Acyl-coenzyme A thioesterase 2, mitochondrial (Acyl-CoA thioesterase 2) (EC 3.1.2.2) (Acyl coenzyme A thioester hydrolase) (MTE-I) (Very-long-chain acyl-CoA thioesterase)
[ACOT12 CACH CACH1 STARD15] Acetyl-coenzyme A thioesterase (EC 3.1.2.1) (Acyl-CoA thioester hydrolase 12) (Acyl-coenzyme A thioesterase 12) (Acyl-CoA thioesterase 12) (Cytoplasmic acetyl-CoA hydrolase 1) (CACH-1) (hCACH-1) (START domain-containing protein 15) (StARD15)
[Acot12 Cach Cach1] Acetyl-coenzyme A thioesterase (EC 3.1.2.1) (Acyl-CoA thioester hydrolase 12) (Acyl-coenzyme A thioesterase 12) (Acyl-CoA thioesterase 12) (Cytoplasmic acetyl-CoA hydrolase 1) (CACH-1) (rACH) (rCACH-1)
[Acot12 Cach Cach1] Acetyl-coenzyme A thioesterase (EC 3.1.2.1) (Acyl-CoA thioester hydrolase 12) (Acyl-coenzyme A thioesterase 12) (Acyl-CoA thioesterase 12) (Cytoplasmic acetyl-CoA hydrolase 1) (CACH-1) (mCACH-1)
[THEM4 CTMP] Acyl-coenzyme A thioesterase THEM4 (Acyl-CoA thioesterase THEM4) (EC 3.1.2.2) (Carboxyl-terminal modulator protein) (Thioesterase superfamily member 4)
[tesA apeA pldC b0494 JW0483] Thioesterase 1/protease 1/lysophospholipase L1 (TAP) (Acyl-CoA thioesterase 1) (TESA) (EC 3.1.2.2) (Acyl-CoA thioesterase I) (Arylesterase) (EC 3.1.1.2) (Lysophospholipase L1) (EC 3.1.1.5) (Oleoyl-[acyl-carrier-protein] hydrolase) (EC 3.1.2.14) (Phospholipid degradation C) (Pldc) (Protease 1) (EC 3.4.21.-) (Protease I) (Thioesterase I/protease I) (TEP-I)
[tesA c0615] Thioesterase 1/protease 1/lysophospholipase L1 (TAP) (Acyl-CoA thioesterase 1) (TESA) (EC 3.1.2.2) (Acyl-CoA thioesterase I) (Arylesterase) (EC 3.1.1.2) (Lysophospholipase L1) (EC 3.1.1.5) (Oleoyl-[acyl-carrier-protein] hydrolase) (EC 3.1.2.14) (Phospholipid degradation C) (Pldc) (Protease 1) (EC 3.4.21.-) (Protease I) (Thioesterase I/protease I) (TEP-I)
[ACOX1 ACOX] Peroxisomal acyl-coenzyme A oxidase 1 (AOX) (EC 1.3.3.6) (Palmitoyl-CoA oxidase) (Straight-chain acyl-CoA oxidase) (SCOX) [Cleaved into: Peroxisomal acyl-CoA oxidase 1, A chain; Peroxisomal acyl-CoA oxidase 1, B chain; Peroxisomal acyl-CoA oxidase 1, C chain]
[BAAT] Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Glycine N-choloyltransferase) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2)
[Baat] Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Glycine N-choloyltransferase) (Kan-1) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2)
[Baat] Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Glycine N-choloyltransferase) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2)
[atnM ANIA_07873] Fatty acid synthase beta subunit aflB (EC 2.3.1.86) (Aspercryptin biosynthesis cluster protein M) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39); S-acyl fatty acid synthase thioesterase (EC 3.1.2.14)]
[ACOX2] Peroxisomal acyl-coenzyme A oxidase 2 (EC 1.17.99.3) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCA-CoA oxidase) (THCCox)
[ACX4 G6 At3g51840 ATEM1.9] Acyl-coenzyme A oxidase 4, peroxisomal (AOX 4) (EC 1.3.3.6) (G6p) (Short-chain acyl-CoA oxidase) (AtCX4) (AtG6) (SAOX)
[] 4-hydroxybenzoyl-CoA thioesterase (EC 3.1.2.23)
[Acsm1 Bucs1 Lae Macs1] Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 1) (Butyrate--CoA ligase 1) (Butyryl-coenzyme A synthetase 1) (Lipoate-activating enzyme) (Middle-chain acyl-CoA synthetase 1)
[menI ydiI b1686 JW1676] 1,4-dihydroxy-2-naphthoyl-CoA hydrolase (DHNA-CoA hydrolase) (EC 3.1.2.28) (DHNA-CoA thioesterase)
[ACSM1 BUCS1 LAE MACS1] Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 1) (Butyrate--CoA ligase 1) (Butyryl-coenzyme A synthetase 1) (Lipoate-activating enzyme) (Middle-chain acyl-CoA synthetase 1) (XL-III) (Xenobiotic/medium-chain fatty acid:CoA ligase XL-3) (XM-ligase 3)
[Acsm3 Sa Sah] Acyl-coenzyme A synthetase ACSM3, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 3) (Butyrate--CoA ligase 3) (Butyryl-coenzyme A synthetase 3) (Middle-chain acyl-CoA synthetase 3) (Protein SA homolog)
[ACSM2A ACSM2 MACS2] Acyl-coenzyme A synthetase ACSM2A, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 2A) (Butyrate--CoA ligase 2A) (Butyryl-coenzyme A synthetase 2A) (Middle-chain acyl-CoA synthetase 2A)
[PPT2] Lysosomal thioesterase PPT2 (PPT-2) (EC 3.1.2.-) (S-thioesterase G14)
[ACSM2B ACSM2 HYST1046] Acyl-coenzyme A synthetase ACSM2B, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 2B) (Butyrate--CoA ligase 2B) (Butyryl-coenzyme A synthetase 2B) (Middle-chain acyl-CoA synthetase 2B) (Xenobiotic/medium-chain fatty acid-CoA ligase HXM-A)
[Lypla1 Apt1 Pla1a] Acyl-protein thioesterase 1 (APT-1) (EC 3.1.2.-) (Lysophospholipase 1) (Lysophospholipase I) (LPL-I) (LysoPLA I)
[LYPLA1 APT1 LPL1] Acyl-protein thioesterase 1 (APT-1) (hAPT1) (EC 3.1.2.-) (Lysophospholipase 1) (Lysophospholipase I) (LPL-I) (LysoPLA I)
[ACX3 At1g06290 F9P14.15 F9P14_11 T2D23.1] Acyl-coenzyme A oxidase 3, peroxisomal (AOX 3) (Acyl-CoA oxidase 3) (EC 1.3.3.6) (Medium-chain acyl-CoA oxidase) (AtCX3)

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