Characterization of Cfa1, a monofunctional acyl carrier protein involved in the biosynthesis of the phytotoxin coronatine.
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ABSTRACT:
SUBMITTER: Seidle H
PROVIDER: S-EPMC412169 | biostudies-literature | 2004 Apr
REPOSITORIES: biostudies-literature
Publications
Characterization of Cfa1, a monofunctional acyl carrier protein involved in the biosynthesis of the phytotoxin coronatine.
Seidle Heather H Rangaswamy Vidhya V Couch Robin R Bender Carol L CL Parry Ronald J RJ
Journal of bacteriology 20040401 8
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. ...[more]
Similar Datasets
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