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EC 6.2.1.46 Details
show Brenda entryEC number
6.2.1.46
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)
Comment
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.
History
created 2015
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1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.14.14.2 created 1972, deleted 1976 1.14.14.4 created 2000, deleted 2002
