In enzymology, an anthranilate—CoA ligase (EC 6.2.1.32) is an enzyme that catalyzes the chemical reaction
Anthranilate—CoA ligase | |||||||||
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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 | ||||||||
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- 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
edit- 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.