ADP-dependent short-chain-acyl-CoA hydrolase | |||||||||
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Identifiers | |||||||||
EC no. | 3.1.2.18 | ||||||||
CAS no. | 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 / QuickGO | ||||||||
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The enzyme ADP-dependent short-chain-acyl-CoA hydrolase (EC 3.1.2.18) 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 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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