EC number:3.1.2.1
| ID: | 3.1.2.1 |
|---|---|
| Description: | Acetyl-CoA hydrolase. |
| Alternative Name: |
Acetyl-CoA deacylase. Acetyl-CoA acylase. |
| Cath: | 3.10.129.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.1.2.1 |
| BRENDA Enzyme Link: | BRENDA 3.1.2.1 |
| KEGG Enzyme Link: | KEGG3.1.2.1 |
| BioCyc Enzyme Link: | BioCyc 3.1.2.1 |
| ExPASy Enzyme Link: | ExPASy3.1.2.1 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.2.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.2.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.2.1 |
| IntEnz Enzyme Link: | IntEnz 3.1.2.1 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.2.1 |
| RHEA:20289 | acetyl-CoA + H2O = acetate + CoA + H(+) |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[*:3])-[S;H0;+0:4]-[*:5].[OH2;+0:6]>>[*:5]-[SH;+0:4].[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structural basis for regulation of the human acetyl-CoA thioesterase 12 and interactions with the steroidogenic acute regulatory protein-related lipid transfer (START) domain. | Swarbrick CM, Roman N, Cowieson N, Patterson EI, Nanson J, Siponen MI, Berglund H, Lehtiö L, Forwood JK | 2014 Aug 29 | 25002576 |
| Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase. | Suematsu N, Isohashi F | 2006 | 16951743 |
| 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 |
| Demonstration of dimethylnonanoyl-CoA thioesterase activity in rat liver peroxisomes followed by purification and molecular cloning of the thioesterase involved. | Ofman R, el Mrabet L, Dacremont G, Spijer D, Wanders RJ | 2002 Jan 18 | 11785945 |