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ENZYME entry: EC 6.2.1.46

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 + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] <=> AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
Comment(s)
  • 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.
Cross-references
BRENDA6.2.1.46
EC2PDB6.2.1.46
ExplorEnz6.2.1.46
PRIAM enzyme-specific profiles6.2.1.46
KEGG Ligand Database for Enzyme Nomenclature6.2.1.46
IUBMB Enzyme Nomenclature6.2.1.46
IntEnz6.2.1.46
MEDLINEFind literature relating to 6.2.1.46
MetaCyc6.2.1.46
UniProtKB/Swiss-Prot
Q6TNA5, CMAA_PSESG

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