| Anthranilate—CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.2.1.32 | ||||||||
| CAS no. | 112692-58-7 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
In enzymology, an anthranilate—CoA ligase (EC 6.2.1.32) is an enzyme that catalyzes the chemical reaction
- ATP + anthranilate + CoA AMP + diphosphate + anthranilyl-CoA
The 3 substrates of this enzyme are ATP, anthranilate, and CoA, whereas its 3 products are AMP, diphosphate, and anthranilyl-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 anthranilate:CoA ligase (AMP-forming). Other names in common use include anthraniloyl coenzyme A synthetase, 2-aminobenzoate-CoA ligase, 2-aminobenzoate-coenzyme A ligase, and 2-aminobenzoate coenzyme A ligase. This enzyme participates in 3 metabolic pathways: carbazole degradation, benzoate degradation via coa ligation, and acridone alkaloid biosynthesis.
References
- Altenschmidt U, Eckerskorn C, Fuchs G (1990). "Evidence that enzymes of a novel aerobic 2-amino-benzoate metabolism in denitrifying Pseudomonas are coded on a small plasmid". Eur. J. Biochem. 194 (2): 647–53. doi:10.1111/j.1432-1033.1990.tb15664.x. PMID 2176602.