ADP-dependent medium-chain-acyl-CoA hydrolase
| ADP-dependent medium-chain-acyl-CoA hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.2.19 | ||||||||
| CAS number | 63363-75-7 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, an ADP-dependent medium-chain-acyl-CoA hydrolase (EC 3.1.2.19) 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-medium-chain-acyl-CoA hydrolase. Other names in common use include medium-chain acyl coenzyme A hydrolase, medium-chain acyl-CoA hydrolase, medium-chain acyl-thioester hydrolase, medium-chain hydrolase, and myristoyl-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.
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