| Synonyms |
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, HIV-Nef-associated acyl-CoA thioesterase, Peroxisomal acyl-CoA thioesterase 2, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, PTE-1, Peroxisomal long-chain acyl-CoA thioesterase 1, Thioesterase II, hACTE-III, hACTEIII, hTE | ACTEIII, PTE1 |
| Function |
Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:9299485, PubMed:9153233, PubMed:15194431). Displays 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). 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}.; (Microbial infection) May mediate Nef-induced down-regulation of CD4 cell-surface expression (PubMed:9153233). {ECO:0000269|PubMed:9153233}. |
3.0
ACOT8
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chemical modification
chemical modification