Carbon extension in peptidylnucleoside biosynthesis by radical-SAM enzymes

Nikkomycins and polyoxins are antifungal peptidylnucleoside (PN) antibiotics active against human and plant pathogens. Here, we report that during PN biosynthesis in Streptomyces cacaoi and Streptomyces tendae, the C5′-extension of the nucleoside essential for downstream structural diversification i...

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Autores principales: Lilla, Edward A., Yokoyama, Kenichi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5069167/
https://www.ncbi.nlm.nih.gov/pubmed/27642865
http://dx.doi.org/10.1038/nchembio.2187
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author Lilla, Edward A.
Yokoyama, Kenichi
author_facet Lilla, Edward A.
Yokoyama, Kenichi
author_sort Lilla, Edward A.
collection PubMed
description Nikkomycins and polyoxins are antifungal peptidylnucleoside (PN) antibiotics active against human and plant pathogens. Here, we report that during PN biosynthesis in Streptomyces cacaoi and Streptomyces tendae, the C5′-extension of the nucleoside essential for downstream structural diversification is catalyzed by a conserved radical S-adenosyl-L-methionine (SAM) enzyme, PolH or NikJ. This is distinct from the nucleophilic mechanism reported for antibacterial nucleosides and represents a novel mechanism of nucleoside natural product biosynthesis.
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spelling pubmed-50691672017-03-19 Carbon extension in peptidylnucleoside biosynthesis by radical-SAM enzymes Lilla, Edward A. Yokoyama, Kenichi Nat Chem Biol Article Nikkomycins and polyoxins are antifungal peptidylnucleoside (PN) antibiotics active against human and plant pathogens. Here, we report that during PN biosynthesis in Streptomyces cacaoi and Streptomyces tendae, the C5′-extension of the nucleoside essential for downstream structural diversification is catalyzed by a conserved radical S-adenosyl-L-methionine (SAM) enzyme, PolH or NikJ. This is distinct from the nucleophilic mechanism reported for antibacterial nucleosides and represents a novel mechanism of nucleoside natural product biosynthesis. 2016-09-19 2016-11 /pmc/articles/PMC5069167/ /pubmed/27642865 http://dx.doi.org/10.1038/nchembio.2187 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Lilla, Edward A.
Yokoyama, Kenichi
Carbon extension in peptidylnucleoside biosynthesis by radical-SAM enzymes
title Carbon extension in peptidylnucleoside biosynthesis by radical-SAM enzymes
title_full Carbon extension in peptidylnucleoside biosynthesis by radical-SAM enzymes
title_fullStr Carbon extension in peptidylnucleoside biosynthesis by radical-SAM enzymes
title_full_unstemmed Carbon extension in peptidylnucleoside biosynthesis by radical-SAM enzymes
title_short Carbon extension in peptidylnucleoside biosynthesis by radical-SAM enzymes
title_sort carbon extension in peptidylnucleoside biosynthesis by radical-sam enzymes
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5069167/
https://www.ncbi.nlm.nih.gov/pubmed/27642865
http://dx.doi.org/10.1038/nchembio.2187
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