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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...

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Detalles Bibliográficos
Autores principales: Biswas, Ansuman, Thattai, Mukund
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2020
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.
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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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