Benzoate—CoA ligase
| Benzoate—CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In
- ATP + benzoate + CoA AMP + diphosphate + benzoyl-CoA
The 3
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
.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. .
- Schennen U, Braun K, Knackmuss HJ (1985). "Anaerobic degradation of 2-fluorobenzoate by benzoate-degrading, denitrifying bacteria". J. Bacteriol. 161 (1): 321–5. PMID 2857161.
