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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2021
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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. |
format | Online Article Text |
id | pubmed-7933479 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
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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