Sublancin is not a lantibiotic but an S-linked glycopeptide

Sublancin is shown to be an S-linked glycopeptide containing a glucose attached to a Cys residue, establishing a new post-translational modification. The activity of the S-glycosyl transferase was reconstituted in vitro and the enzyme is shown to have relaxed substrate specificity allowing the prepa...

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Autores principales: Oman, Trent J., Boettcher, John M., Wang, Huan, Okalibe, Xenia N., van der Donk, Wilfred A.
Formato: Texto
Lenguaje:English
Publicado: 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3060661/
https://www.ncbi.nlm.nih.gov/pubmed/21196935
http://dx.doi.org/10.1038/nchembio.509
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author Oman, Trent J.
Boettcher, John M.
Wang, Huan
Okalibe, Xenia N.
van der Donk, Wilfred A.
author_facet Oman, Trent J.
Boettcher, John M.
Wang, Huan
Okalibe, Xenia N.
van der Donk, Wilfred A.
author_sort Oman, Trent J.
collection PubMed
description Sublancin is shown to be an S-linked glycopeptide containing a glucose attached to a Cys residue, establishing a new post-translational modification. The activity of the S-glycosyl transferase was reconstituted in vitro and the enzyme is shown to have relaxed substrate specificity allowing the preparation of analogs of sublancin. Glycosylation is essential for its antimicrobial activity.
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spelling pubmed-30606612011-08-01 Sublancin is not a lantibiotic but an S-linked glycopeptide Oman, Trent J. Boettcher, John M. Wang, Huan Okalibe, Xenia N. van der Donk, Wilfred A. Nat Chem Biol Article Sublancin is shown to be an S-linked glycopeptide containing a glucose attached to a Cys residue, establishing a new post-translational modification. The activity of the S-glycosyl transferase was reconstituted in vitro and the enzyme is shown to have relaxed substrate specificity allowing the preparation of analogs of sublancin. Glycosylation is essential for its antimicrobial activity. 2011-01-02 2011-02 /pmc/articles/PMC3060661/ /pubmed/21196935 http://dx.doi.org/10.1038/nchembio.509 Text en Users may view, print, copy, download and 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
Oman, Trent J.
Boettcher, John M.
Wang, Huan
Okalibe, Xenia N.
van der Donk, Wilfred A.
Sublancin is not a lantibiotic but an S-linked glycopeptide
title Sublancin is not a lantibiotic but an S-linked glycopeptide
title_full Sublancin is not a lantibiotic but an S-linked glycopeptide
title_fullStr Sublancin is not a lantibiotic but an S-linked glycopeptide
title_full_unstemmed Sublancin is not a lantibiotic but an S-linked glycopeptide
title_short Sublancin is not a lantibiotic but an S-linked glycopeptide
title_sort sublancin is not a lantibiotic but an s-linked glycopeptide
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3060661/
https://www.ncbi.nlm.nih.gov/pubmed/21196935
http://dx.doi.org/10.1038/nchembio.509
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AT vanderdonkwilfreda sublancinisnotalantibioticbutanslinkedglycopeptide

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