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Polysaccharide Biosynthesis: Glycosyltransferases and Their Complexes

Glycosyltransferases (GTs) are enzymes that catalyze reactions attaching an activated sugar to an acceptor substrate, which may be a polysaccharide, peptide, lipid, or small molecule. In the past decade, notable progress has been made in revealing and cloning genes encoding polysaccharide-synthesizi...

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Detalles Bibliográficos
Autores principales: Zabotina, Olga A., Zhang, Ning, Weerts, Richard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7933479/
https://www.ncbi.nlm.nih.gov/pubmed/33679837
http://dx.doi.org/10.3389/fpls.2021.625307
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author Zabotina, Olga A.
Zhang, Ning
Weerts, Richard
author_facet Zabotina, Olga A.
Zhang, Ning
Weerts, Richard
author_sort Zabotina, Olga A.
collection PubMed
description Glycosyltransferases (GTs) are enzymes that catalyze reactions attaching an activated sugar to an acceptor substrate, which may be a polysaccharide, peptide, lipid, or small molecule. In the past decade, notable progress has been made in revealing and cloning genes encoding polysaccharide-synthesizing GTs. However, the vast majority of GTs remain structurally and functionally uncharacterized. The mechanism by which they are organized in the Golgi membrane, where they synthesize complex, highly branched polysaccharide structures with high efficiency and fidelity, is also mostly unknown. This review will focus on current knowledge about plant polysaccharide-synthesizing GTs, specifically focusing on protein-protein interactions and the formation of multiprotein complexes.
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spelling pubmed-79334792021-03-06 Polysaccharide Biosynthesis: Glycosyltransferases and Their Complexes Zabotina, Olga A. Zhang, Ning Weerts, Richard Front Plant Sci Plant Science Glycosyltransferases (GTs) are enzymes that catalyze reactions attaching an activated sugar to an acceptor substrate, which may be a polysaccharide, peptide, lipid, or small molecule. In the past decade, notable progress has been made in revealing and cloning genes encoding polysaccharide-synthesizing GTs. However, the vast majority of GTs remain structurally and functionally uncharacterized. The mechanism by which they are organized in the Golgi membrane, where they synthesize complex, highly branched polysaccharide structures with high efficiency and fidelity, is also mostly unknown. This review will focus on current knowledge about plant polysaccharide-synthesizing GTs, specifically focusing on protein-protein interactions and the formation of multiprotein complexes. Frontiers Media S.A. 2021-02-19 /pmc/articles/PMC7933479/ /pubmed/33679837 http://dx.doi.org/10.3389/fpls.2021.625307 Text en Copyright © 2021 Zabotina, Zhang and Weerts. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Zabotina, Olga A.
Zhang, Ning
Weerts, Richard
Polysaccharide Biosynthesis: Glycosyltransferases and Their Complexes
title Polysaccharide Biosynthesis: Glycosyltransferases and Their Complexes
title_full Polysaccharide Biosynthesis: Glycosyltransferases and Their Complexes
title_fullStr Polysaccharide Biosynthesis: Glycosyltransferases and Their Complexes
title_full_unstemmed Polysaccharide Biosynthesis: Glycosyltransferases and Their Complexes
title_short Polysaccharide Biosynthesis: Glycosyltransferases and Their Complexes
title_sort polysaccharide biosynthesis: glycosyltransferases and their complexes
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7933479/
https://www.ncbi.nlm.nih.gov/pubmed/33679837
http://dx.doi.org/10.3389/fpls.2021.625307
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