| 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
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2V7B.
References
- 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.
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