Structural and mechanistic basis for a novel mode of glycosyltransferase inhibition

Glycosyltransferases are carbohydrate-active enzymes with essential roles in numerous important biological processes. We have developed a novel donor analogue for galactosyltransferases which locks a representative target enzyme in a catalytically inactive conformation, thus almost completely abolis...

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Detalles Bibliográficos
Autores principales: Pesnot, Thomas, Jørgensen, Rene, Palcic, Monica M., Wagner, Gerd K.
Formato: Texto
Lenguaje:English
Publicado: 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2883747/
https://www.ncbi.nlm.nih.gov/pubmed/20364127
http://dx.doi.org/10.1038/nchembio.343
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author Pesnot, Thomas
Jørgensen, Rene
Palcic, Monica M.
Wagner, Gerd K.
author_facet Pesnot, Thomas
Jørgensen, Rene
Palcic, Monica M.
Wagner, Gerd K.
author_sort Pesnot, Thomas
collection PubMed
description Glycosyltransferases are carbohydrate-active enzymes with essential roles in numerous important biological processes. We have developed a novel donor analogue for galactosyltransferases which locks a representative target enzyme in a catalytically inactive conformation, thus almost completely abolishing sugar transfer. Results with other galactosyltransferases suggest that this novel and unique mode of glycosyltransferase inhibition is, very likely, generally applicable to other members of this very important enzyme family also.
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spelling pubmed-28837472010-11-01 Structural and mechanistic basis for a novel mode of glycosyltransferase inhibition Pesnot, Thomas Jørgensen, Rene Palcic, Monica M. Wagner, Gerd K. Nat Chem Biol Article Glycosyltransferases are carbohydrate-active enzymes with essential roles in numerous important biological processes. We have developed a novel donor analogue for galactosyltransferases which locks a representative target enzyme in a catalytically inactive conformation, thus almost completely abolishing sugar transfer. Results with other galactosyltransferases suggest that this novel and unique mode of glycosyltransferase inhibition is, very likely, generally applicable to other members of this very important enzyme family also. 2010-04-04 2010-05 /pmc/articles/PMC2883747/ /pubmed/20364127 http://dx.doi.org/10.1038/nchembio.343 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
Pesnot, Thomas
Jørgensen, Rene
Palcic, Monica M.
Wagner, Gerd K.
Structural and mechanistic basis for a novel mode of glycosyltransferase inhibition
title Structural and mechanistic basis for a novel mode of glycosyltransferase inhibition
title_full Structural and mechanistic basis for a novel mode of glycosyltransferase inhibition
title_fullStr Structural and mechanistic basis for a novel mode of glycosyltransferase inhibition
title_full_unstemmed Structural and mechanistic basis for a novel mode of glycosyltransferase inhibition
title_short Structural and mechanistic basis for a novel mode of glycosyltransferase inhibition
title_sort structural and mechanistic basis for a novel mode of glycosyltransferase inhibition
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2883747/
https://www.ncbi.nlm.nih.gov/pubmed/20364127
http://dx.doi.org/10.1038/nchembio.343
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AT wagnergerdk structuralandmechanisticbasisforanovelmodeofglycosyltransferaseinhibition

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