Description
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.
Form
Liquid or lyophilized powder
Storage
Store it at +4 ºC for short term. For long term storage, store it at -20 ºC~-80 ºC.
Reaction
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] = AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
Notes
This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications.