ADP-dependent short-chain-acyl-CoA hydrolase
| ADP-dependent short-chain-acyl-CoA hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.2.18 | ||||||||
| CAS number | 117698-16-5 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, an ADP-dependent short-chain-acyl-CoA hydrolase (EC 3.1.2.18) 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 ADP-dependent-short-chain-acyl-CoA hydrolase. Other names in common use include short-chain acyl coenzyme A hydrolase, propionyl coenzyme A hydrolase, propionyl-CoA hydrolase, propionyl-CoA thioesterase, short-chain acyl-CoA hydrolase, and short-chain acyl-CoA thioesterase. It employs one cofactor, ADP. At least one compound, NADH is known to inhibit this enzyme.
References
- Alexson SE, Nedergaard J (1988). "A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria". J. Biol. Chem. 263 (27): 13564–71. PMID 2901416.
- 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.
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