The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: L-allo-isoleucine—holo-[CmaA peptidyl-carrier protein] ligase
Reaction: ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] = AMP + diphosphate + L-allo-isoleucyl-[CmaA peptidyl-carrier protein]
Other name(s): CmaA
Systematic name: L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase (AMP-forming)
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Couch, R., O'Connor, S.E., Seidle, H., Walsh, C.T. and Parry, R. Characterization of CmaA, an adenylation-thiolation didomain enzyme involved in the biosynthesis of coronatine. J. Bacteriol. 186 (2004) 35–42. [DOI] [PMID: 14679222]
[EC created 2015]

Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald