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

for references in articles please use BRENDA:EC6.2.1.46
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IUBMB Comments
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.
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The expected taxonomic range for this enzyme is: Pseudomonas syringae group
CmaA, CmaE, L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase, more
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] = AMP + diphosphate + L-allo-isoleucyl-[CmaA peptidyl-carrier protein]
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