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ENZYME entry: EC

Accepted Name
L-allo-isoleucine--holo-[CmaA peptidyl-carrier protein] ligase
Alternative Name(s)
L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase
Reaction catalysed
ATP + holo-[CmaA peptidyl-carrier protein] + L-alloisoleucine <=> AMP + diphosphate + L-alloisoleucyl-[CmaA peptidyl-carrier protein]
  • This two-domain protein from the bacterium Pseudomonas syringae contains an adenylation domain (A domain) and a thiolation domain (T domain).
  • It catalyzes 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.
PRIAM enzyme-specific profiles6.2.1.46
KEGG Ligand Database for Enzyme Nomenclature6.2.1.46
IUBMB Enzyme Nomenclature6.2.1.46
MEDLINEFind literature relating to
Rhea expert-curated reactions6.2.1.46

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