Benzoate—CoA ligase
| Benzoate—CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.2.1.25 | ||||||||
| CAS no. | 95329-17-2 | ||||||||
| 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, a benzoate—CoA ligase (EC 6.2.1.25) is an enzyme that catalyzes the chemical reaction
- ATP + benzoate + CoA AMP + diphosphate + benzoyl-CoA
The 3 substrates of this enzyme are ATP, benzoate, and CoA, whereas its 3 products are AMP, diphosphate, and benzoyl-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 benzoate:CoA ligase (AMP-forming). Other names in common use include benzoate-coenzyme A ligase, benzoyl-coenzyme A synthetase, and benzoyl CoA synthetase (AMP forming). This enzyme participates in benzoate degradation via coa ligation.
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2V7B.
References
[edit]- Hutber GN; Ribbons DW (1983). "Involvement of coenzyme-A esters in the metabolism of benzoate and cyclohexanecarboxylate by Rhodopseudomonas palustris". J. Gen. Microbiol. 129 (8): 2413–2420. doi:10.1099/00221287-129-8-2413.
- Schennen U, Braun K, Knackmuss HJ (1985). "Anaerobic degradation of 2-fluorobenzoate by benzoate-degrading, denitrifying bacteria". J. Bacteriol. 161 (1): 321–5. doi:10.1128/JB.161.1.321-325.1985. PMC 214874. PMID 2857161.
