EC number:3.1.2.19
| ID: | 3.1.2.19 |
|---|---|
| Description: | ADP-dependent medium-chain-acyl-CoA hydrolase. |
| Cath: | 3.10.129.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.1.2.19 |
| BRENDA Enzyme Link: | BRENDA 3.1.2.19 |
| KEGG Enzyme Link: | KEGG3.1.2.19 |
| BioCyc Enzyme Link: | BioCyc 3.1.2.19 |
| ExPASy Enzyme Link: | ExPASy3.1.2.19 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.2.19 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.2.19 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.2.19 |
| IntEnz Enzyme Link: | IntEnz 3.1.2.19 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.2.19 |
| RHEA:16781 | an acyl-CoA + H2O = a fatty acid + CoA + H(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[S;H0;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[SH;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Peroxisome proliferator-induced acyl-CoA thioesterase from rat liver cytosol: molecular cloning and functional expression in Chinese hamster ovary cells. | Engberg ST, Aoyama T, Alexson SE, Hashimoto T, Svensson LT | 1997 Apr 15 | 9163348 |
| Roles of Ser101, Asp236, and His237 in catalysis of thioesterase II and of the C-terminal region of the enzyme in its interaction with fatty acid synthase. | Tai MH, Chirala SS, Wakil SJ | 1993 Mar 1 | 8446599 |
| Purification and properties of long-chain acyl-CoA hydrolases from the liver cytosol of rats treated with peroxisome proliferator. | Yamada J, Matsumoto I, Furihata T, Sakuma M, Suga T | 1994 Jan | 7906114 |
| The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family. | Zhao H, Martin BM, Bisoffi M, Dunaway-Mariano D | 2009 Jun 23 | 19453107 |
| Molecular cloning and characterization of two mouse peroxisome proliferator-activated receptor alpha (PPARalpha)-regulated peroxisomal acyl-CoA thioesterases. | Westin MA, Alexson SE, Hunt MC | 2004 May 21 | 15007068 |
| Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. | Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE | 2006 Sep | 16940157 |
| Characterization of an acyl-coA thioesterase that functions as a major regulator of peroxisomal lipid metabolism. | Hunt MC, Solaas K, Kase BF, Alexson SE | 2002 Jan 11 | 11673457 |