EC - L-allo-isoleucine—holo-[CmaA peptidyl-carrier protein] ligase

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IntEnz Enzyme Nomenclature


Accepted name:
L-allo-isoleucine—holo-[CmaA peptidyl-carrier protein] ligase
Other names:
L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase
Systematic name:
L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase (AMP-forming)



This two-domain protein from the bacterium Pseudomonas syringae contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyses the adenylation of L-allo-isoleucine and its attachment to the T domain. The enzyme is involved in the biosynthesis of the toxin coronatine, which mimics the plant hormone jasmonic acid isoleucine. Coronatine promotes opening of the plant stomata allowing bacterial invasion, which is followed by bacterial growth in the apoplast, systemic susceptibility, and disease.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Couch, R., O'Connor, S. E., Seidle, H., Walsh, C. T., Parry, R.
    Characterization of CmaA, an adenylation-thiolation didomain enzyme involved in the biosynthesis of coronatine.
    J. Bacteriol. 186 : 35-42 (2004). [PMID: 14679222]

[EC created 2015]