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Information on EC 6.2.1.46 - L-allo-isoleucine-holo-[CmaA peptidyl-carrier protein] ligase

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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
Synonyms
CmaA, CmaE, L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] = AMP + diphosphate + L-allo-isoleucyl-[CmaA peptidyl-carrier protein]
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