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Promiscuity and specificity of eukaryotic glycosyltransferases
Glycosyltransferases are a large family of enzymes responsible for covalently linking sugar monosaccharides to a variety of organic substrates. These enzymes drive the synthesis of complex oligosaccharides known as glycans, which play key roles in inter-cellular interactions across all the kingdoms...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7329348/ https://www.ncbi.nlm.nih.gov/pubmed/32539082 http://dx.doi.org/10.1042/BST20190651 |
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author | Biswas, Ansuman Thattai, Mukund |
author_facet | Biswas, Ansuman Thattai, Mukund |
author_sort | Biswas, Ansuman |
collection | PubMed |
description | Glycosyltransferases are a large family of enzymes responsible for covalently linking sugar monosaccharides to a variety of organic substrates. These enzymes drive the synthesis of complex oligosaccharides known as glycans, which play key roles in inter-cellular interactions across all the kingdoms of life; they also catalyze sugar attachment during the synthesis of small-molecule metabolites such as plant flavonoids. A given glycosyltransferase enzyme is typically responsible for attaching a specific donor monosaccharide, via a specific glycosidic linkage, to a specific moiety on the acceptor substrate. However these enzymes are often promiscuous, able catalyze linkages between a variety of donors and acceptors. In this review we discuss distinct classes of glycosyltransferase promiscuity, each illustrated by enzymatic examples from small-molecule or glycan synthesis. We highlight the physical causes of promiscuity, and its biochemical consequences. Structural studies of glycosyltransferases involved in glycan synthesis show that they make specific contacts with ‘recognition motifs’ that are much smaller than the full oligosaccharide substrate. There is a wide range in the sizes of glycosyltransferase recognition motifs: highly promiscuous enzymes recognize monosaccharide or disaccharide motifs across multiple oligosaccharides, while highly specific enzymes recognize large, complex motifs found on few oligosaccharides. In eukaryotes, the localization of glycosyltransferases within compartments of the Golgi apparatus may play a role in mitigating the glycan variability caused by enzyme promiscuity. |
format | Online Article Text |
id | pubmed-7329348 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-73293482020-07-13 Promiscuity and specificity of eukaryotic glycosyltransferases Biswas, Ansuman Thattai, Mukund Biochem Soc Trans Review Articles Glycosyltransferases are a large family of enzymes responsible for covalently linking sugar monosaccharides to a variety of organic substrates. These enzymes drive the synthesis of complex oligosaccharides known as glycans, which play key roles in inter-cellular interactions across all the kingdoms of life; they also catalyze sugar attachment during the synthesis of small-molecule metabolites such as plant flavonoids. A given glycosyltransferase enzyme is typically responsible for attaching a specific donor monosaccharide, via a specific glycosidic linkage, to a specific moiety on the acceptor substrate. However these enzymes are often promiscuous, able catalyze linkages between a variety of donors and acceptors. In this review we discuss distinct classes of glycosyltransferase promiscuity, each illustrated by enzymatic examples from small-molecule or glycan synthesis. We highlight the physical causes of promiscuity, and its biochemical consequences. Structural studies of glycosyltransferases involved in glycan synthesis show that they make specific contacts with ‘recognition motifs’ that are much smaller than the full oligosaccharide substrate. There is a wide range in the sizes of glycosyltransferase recognition motifs: highly promiscuous enzymes recognize monosaccharide or disaccharide motifs across multiple oligosaccharides, while highly specific enzymes recognize large, complex motifs found on few oligosaccharides. In eukaryotes, the localization of glycosyltransferases within compartments of the Golgi apparatus may play a role in mitigating the glycan variability caused by enzyme promiscuity. Portland Press Ltd. 2020-06-30 2020-06-15 /pmc/articles/PMC7329348/ /pubmed/32539082 http://dx.doi.org/10.1042/BST20190651 Text en © 2020 The Author(s) https://creativecommons.org/licenses/by/4.0/ This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Review Articles Biswas, Ansuman Thattai, Mukund Promiscuity and specificity of eukaryotic glycosyltransferases |
title | Promiscuity and specificity of eukaryotic glycosyltransferases |
title_full | Promiscuity and specificity of eukaryotic glycosyltransferases |
title_fullStr | Promiscuity and specificity of eukaryotic glycosyltransferases |
title_full_unstemmed | Promiscuity and specificity of eukaryotic glycosyltransferases |
title_short | Promiscuity and specificity of eukaryotic glycosyltransferases |
title_sort | promiscuity and specificity of eukaryotic glycosyltransferases |
topic | Review Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7329348/ https://www.ncbi.nlm.nih.gov/pubmed/32539082 http://dx.doi.org/10.1042/BST20190651 |
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