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- W1963995384 abstract "Paenibacillus polymyxa PKB1 produces fusaricidins, a family of lipopeptide antibiotics that strongly inhibits the growth of many plant pathogenic fungi. The fusaricidin biosynthetic gene cluster was cloned and sequenced, and it spans 32.4 kb, including an open reading frame (fusA) encoding a six-module nonribosomal peptide synthetase. The second, fourth, and fifth modules of fusaricidin synthetase each contain an epimerization domain, consistent with the structure of fusaricidins. However, no epimerization domain is found in the sixth module, corresponding to d-Ala. This sixth adenylation domain was produced at a high level in Escherichia coli and is shown to activate d-Ala specifically, providing evidence for direct activation of a d-amino acid by a prokaryotic peptide synthetase. The fusaricidin gene cluster also includes genes involved in the biosynthesis of the lipid moiety, but no genes for resistance, regulation, or transport functions were encountered." @default.
- W1963995384 created "2016-06-24" @default.
- W1963995384 creator A5004247993 @default.
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- W1963995384 date "2008-02-01" @default.
- W1963995384 modified "2023-10-16" @default.
- W1963995384 title "Nonribosomal Biosynthesis of Fusaricidins by Paenibacillus polymyxa PKB1 Involves Direct Activation of a d-Amino Acid" @default.
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- W1963995384 doi "https://doi.org/10.1016/j.chembiol.2007.12.014" @default.
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