NRPS Substrate Promiscuity Diversifies the Xenematides

[Image: see text] 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 xene...

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Autores principales: Crawford, Jason M., Portmann, Cyril, Kontnik, Renee, Walsh, Christopher T., Clardy, Jon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2011
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3184645/
https://www.ncbi.nlm.nih.gov/pubmed/21888371
http://dx.doi.org/10.1021/ol2020237
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author Crawford, Jason M.
Portmann, Cyril
Kontnik, Renee
Walsh, Christopher T.
Clardy, Jon
author_facet Crawford, Jason M.
Portmann, Cyril
Kontnik, Renee
Walsh, Christopher T.
Clardy, Jon
author_sort Crawford, Jason M.
collection PubMed
description [Image: see text] 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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spelling pubmed-31846452011-10-03 NRPS Substrate Promiscuity Diversifies the Xenematides Crawford, Jason M. Portmann, Cyril Kontnik, Renee Walsh, Christopher T. Clardy, Jon Org Lett [Image: see text] 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. American Chemical Society 2011-09-02 2011-10-07 /pmc/articles/PMC3184645/ /pubmed/21888371 http://dx.doi.org/10.1021/ol2020237 Text en Copyright © 2011 American Chemical Society http://pubs.acs.org This is an open-access article distributed under the ACS AuthorChoice Terms & Conditions. Any use of this article, must conform to the terms of that license which are available at http://pubs.acs.org.
spellingShingle Crawford, Jason M.
Portmann, Cyril
Kontnik, Renee
Walsh, Christopher T.
Clardy, Jon
NRPS Substrate Promiscuity Diversifies the Xenematides
title NRPS Substrate Promiscuity Diversifies the Xenematides
title_full NRPS Substrate Promiscuity Diversifies the Xenematides
title_fullStr NRPS Substrate Promiscuity Diversifies the Xenematides
title_full_unstemmed NRPS Substrate Promiscuity Diversifies the Xenematides
title_short NRPS Substrate Promiscuity Diversifies the Xenematides
title_sort nrps substrate promiscuity diversifies the xenematides
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3184645/
https://www.ncbi.nlm.nih.gov/pubmed/21888371
http://dx.doi.org/10.1021/ol2020237
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