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 | ||||||||
| |||||||||
In enzymology, an acyl-CoA hydrolase (EC 3.1.2.20) is an enzyme that catalyzes the chemical reaction
- acyl-CoA + H2O CoA + a carboxylate
Thus, the two substrates of this enzyme are acyl-CoA and H2O, whereas its two products are CoA and 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[]
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1Y7U and 2GVH.
References[]
- 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.
Categories:
- EC 3.1.2
- Enzymes of known structure
- EC 3.1 stubs