NRPS Substrate Promiscuity Diversifies the Xenematides
Author(s) -
Jason M. Crawford,
Cyril Portmann,
Renee Kontnik,
Christopher T. Walsh,
Jon Clardy
Publication year - 2011
Publication title -
organic letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.94
H-Index - 239
eISSN - 1523-7060
pISSN - 1523-7052
DOI - 10.1021/ol2020237
Subject(s) - nonribosomal peptide , adenylylation , chemistry , mutant , moiety , wild type , peptide , promiscuity , stereochemistry , biochemistry , biosynthesis , enzyme , biology , gene , ecology
Xenematide, a cyclic depsipeptide antibiotic produced by Xenorhabdus nematophila, had a candidate nonribosomal peptide synthetase (NRPS) with atypical features. Differential metabolite analysis between a mutant and wildtype validated that this stand-alone NRPS was required for xenematide production, and further analysis led to a series of new xenematide derivatives encoded by the same NRPS. Our results indicate that adenylation domain promiscuity and relaxed downstream processing in the X. nematophila NRPS provide a conduit for xenematide diversification.
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