In enzymology, a dicarboxylate—CoA ligase (EC 6.2.1.23) is an enzyme that catalyzes the chemical reaction
| Dicarboxylate—CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.2.1.23 | ||||||||
| CAS no. | 99332-77-1 | ||||||||
| 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 | ||||||||
| |||||||||
- ATP + an alphaomega-dicarboxylic acid + CoA AMP + diphosphate + an omega-carboxyacyl-CoA
The 3 substrates of this enzyme are ATP, alphaomega-dicarboxylic acid, and CoA, whereas its 3 products are AMP, diphosphate, and omega-carboxyacyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is omega-dicarboxylate:CoA ligase (AMP-forming). Other names in common use include carboxylyl-CoA synthetase, and dicarboxylyl-CoA synthetase.
References
edit- Vamecq J, de Hoffmann E, Van Hoof F (1985). "The microsomal dicarboxylyl-CoA synthetase". Biochem. J. 230 (3): 683–93. PMC 1152672. PMID 4062873.
