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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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[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.
Well, that’s interesting to know that Psilotum nudum are known as whisk ferns. Psilotum nudum is the commoner species of the two. While the P. flaccidum is a rare species and is found in the tropical islands. Both the species are usually epiphytic in habit and grow upon tree ferns. These species may also be terrestrial and grow in humus or in the crevices of the rocks.
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