Acyl-CoA hydrolase
| acyl-CoA hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.2.20 | ||||||||
| CAS no. | 37270-64-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme acyl-CoA hydrolase (EC 3.1.2.20) catalyzes the reaction
- acyl-CoA + H2O CoA + a carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is acyl-CoA hydrolase. Other names in common use include acyl coenzyme A thioesterase, acyl-CoA thioesterase, acyl coenzyme A hydrolase, thioesterase B, thioesterase II, and acyl-CoA thioesterase.
Structural studies
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1Y7U and 2GVH.
References
[edit]- Alexson SE, Svensson LT, Nedergaard J (1989). "NADH-sensitive propionyl-CoA hydrolase in brown-adipose-tissue mitochondria of the rat". Biochim. Biophys. Acta. 1005 (1): 13–9. doi:10.1016/0005-2760(89)90025-8. PMID 2570608.
