Characterization of Cfa1, a monofunctional acyl carrier protein involved in the biosynthesis of the phytotoxin coronatine
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Date
2004-04Author
Seidle, Heather
Rangaswamy, Vidhya
Couch, Robin
Bender, Carol L.
Parry, Ronald J.
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Cfa1 was overproduced in Escherichia coli and Pseudomonas syringae, and the degree of 4'-phosphopantetheinylation was determined. The malonyl-coenzyme A:acyl carrier protein transacylase (FabD) of P. syringae was overproduced and shown to catalyze malonylation of Cfa1, suggesting that FabD plays a role in coronatine biosynthesis. Highly purified Cfa1 did not exhibit self-malonylation activity.
Citation
Seidle, H., Rangaswamy, V., Couch, R., Bender, C. L., & Parry, R. J. (2004). Characterization of Cfa1, a monofunctional acyl carrier protein involved in the biosynthesis of the phytotoxin coronatine. Journal of Bacteriology, 186(8), 2499-2503. https://doi.org/10.1128/JB.186.8.2499-2503.2004