Sources of Diversity in Bactobolin Biosynthesis by Burkholderia thailandensis E264

[Image: see text] A series of deletion mutants in the recently identified bactobolin biosynthetic pathway defined the roles of several key biosynthetic enzymes and showed how promiscuity in three enzyme systems allows this cluster to produce multiple products. Studies on the deletion mutants also le...

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Autores principales: Carr, Gavin, Seyedsayamdost, Mohammad R., Chandler, Josephine R., Greenberg, E. Peter, Clardy, Jon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2011
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3111747/
https://www.ncbi.nlm.nih.gov/pubmed/21615115
http://dx.doi.org/10.1021/ol200922s
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author Carr, Gavin
Seyedsayamdost, Mohammad R.
Chandler, Josephine R.
Greenberg, E. Peter
Clardy, Jon
author_facet Carr, Gavin
Seyedsayamdost, Mohammad R.
Chandler, Josephine R.
Greenberg, E. Peter
Clardy, Jon
author_sort Carr, Gavin
collection PubMed
description [Image: see text] A series of deletion mutants in the recently identified bactobolin biosynthetic pathway defined the roles of several key biosynthetic enzymes and showed how promiscuity in three enzyme systems allows this cluster to produce multiple products. Studies on the deletion mutants also led to four new bactobolin analogs that provide additional structure–activity relationships for this interesting antibiotic family.
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spelling pubmed-31117472011-06-10 Sources of Diversity in Bactobolin Biosynthesis by Burkholderia thailandensis E264 Carr, Gavin Seyedsayamdost, Mohammad R. Chandler, Josephine R. Greenberg, E. Peter Clardy, Jon Org Lett [Image: see text] A series of deletion mutants in the recently identified bactobolin biosynthetic pathway defined the roles of several key biosynthetic enzymes and showed how promiscuity in three enzyme systems allows this cluster to produce multiple products. Studies on the deletion mutants also led to four new bactobolin analogs that provide additional structure–activity relationships for this interesting antibiotic family. American Chemical Society 2011-05-26 2011-06-17 /pmc/articles/PMC3111747/ /pubmed/21615115 http://dx.doi.org/10.1021/ol200922s 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 Carr, Gavin
Seyedsayamdost, Mohammad R.
Chandler, Josephine R.
Greenberg, E. Peter
Clardy, Jon
Sources of Diversity in Bactobolin Biosynthesis by Burkholderia thailandensis E264
title Sources of Diversity in Bactobolin Biosynthesis by Burkholderia thailandensis E264
title_full Sources of Diversity in Bactobolin Biosynthesis by Burkholderia thailandensis E264
title_fullStr Sources of Diversity in Bactobolin Biosynthesis by Burkholderia thailandensis E264
title_full_unstemmed Sources of Diversity in Bactobolin Biosynthesis by Burkholderia thailandensis E264
title_short Sources of Diversity in Bactobolin Biosynthesis by Burkholderia thailandensis E264
title_sort sources of diversity in bactobolin biosynthesis by burkholderia thailandensis e264
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3111747/
https://www.ncbi.nlm.nih.gov/pubmed/21615115
http://dx.doi.org/10.1021/ol200922s
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