EC Number   |
Natural Substrates |
|---|
  6.2.1.46 | ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] |
during the biosynthesis of the cyclopropyl amino acid coronamic acid from L-allo-Ile by the phytotoxic Pseudomonas syringae, the aminoacyl group covalently attached to the pantetheinyl arm of CmaA is shuttled to the HS-pantetheinyl arm of the protein CmaD by the aminoacyltransferase CmaE, reversible shuttling process |
| 6.2.1.46 | ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine |
the didomain protein contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyzes the adenylation of L-allo-isoleucine and the attachment of L-allo-isoleucine to the CmaA T domain. The enzyme-bound L-allo-isoleucine serves as the substrate for the later stages of the biosdynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease |
