Cargando…

Bacterial Glycosyltransferases: Challenges and Opportunities of a Highly Diverse Enzyme Class Toward Tailoring Natural Products

The enzyme subclass of glycosyltransferases (GTs; EC 2.4) currently comprises 97 families as specified by CAZy classification. One of their important roles is in the biosynthesis of disaccharides, oligosaccharides, and polysaccharides by catalyzing the transfer of sugar moieties from activated donor...

Descripción completa

Detalles Bibliográficos
Autores principales: Schmid, Jochen, Heider, Dominik, Wendel, Norma J., Sperl, Nadine, Sieber, Volker
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4757703/
https://www.ncbi.nlm.nih.gov/pubmed/26925049
http://dx.doi.org/10.3389/fmicb.2016.00182
_version_ 1782416494125121536
author Schmid, Jochen
Heider, Dominik
Wendel, Norma J.
Sperl, Nadine
Sieber, Volker
author_facet Schmid, Jochen
Heider, Dominik
Wendel, Norma J.
Sperl, Nadine
Sieber, Volker
author_sort Schmid, Jochen
collection PubMed
description The enzyme subclass of glycosyltransferases (GTs; EC 2.4) currently comprises 97 families as specified by CAZy classification. One of their important roles is in the biosynthesis of disaccharides, oligosaccharides, and polysaccharides by catalyzing the transfer of sugar moieties from activated donor molecules to other sugar molecules. In addition GTs also catalyze the transfer of sugar moieties onto aglycons, which is of great relevance for the synthesis of many high value natural products. Bacterial GTs show a higher sequence similarity in comparison to mammalian ones. Even when most GTs are poorly explored, state of the art technologies, such as protein engineering, domain swapping or computational analysis strongly enhance our understanding and utilization of these very promising classes of proteins. This perspective article will focus on bacterial GTs, especially on classification, screening and engineering strategies to alter substrate specificity. The future development in these fields as well as obstacles and challenges will be highlighted and discussed.
format Online
Article
Text
id pubmed-4757703
institution National Center for Biotechnology Information
language English
publishDate 2016
publisher Frontiers Media S.A.
record_format MEDLINE/PubMed
spelling pubmed-47577032016-02-26 Bacterial Glycosyltransferases: Challenges and Opportunities of a Highly Diverse Enzyme Class Toward Tailoring Natural Products Schmid, Jochen Heider, Dominik Wendel, Norma J. Sperl, Nadine Sieber, Volker Front Microbiol Microbiology The enzyme subclass of glycosyltransferases (GTs; EC 2.4) currently comprises 97 families as specified by CAZy classification. One of their important roles is in the biosynthesis of disaccharides, oligosaccharides, and polysaccharides by catalyzing the transfer of sugar moieties from activated donor molecules to other sugar molecules. In addition GTs also catalyze the transfer of sugar moieties onto aglycons, which is of great relevance for the synthesis of many high value natural products. Bacterial GTs show a higher sequence similarity in comparison to mammalian ones. Even when most GTs are poorly explored, state of the art technologies, such as protein engineering, domain swapping or computational analysis strongly enhance our understanding and utilization of these very promising classes of proteins. This perspective article will focus on bacterial GTs, especially on classification, screening and engineering strategies to alter substrate specificity. The future development in these fields as well as obstacles and challenges will be highlighted and discussed. Frontiers Media S.A. 2016-02-18 /pmc/articles/PMC4757703/ /pubmed/26925049 http://dx.doi.org/10.3389/fmicb.2016.00182 Text en Copyright © 2016 Schmid, Heider, Wendel, Sperl and Sieber. http://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) or licensor 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 Microbiology
Schmid, Jochen
Heider, Dominik
Wendel, Norma J.
Sperl, Nadine
Sieber, Volker
Bacterial Glycosyltransferases: Challenges and Opportunities of a Highly Diverse Enzyme Class Toward Tailoring Natural Products
title Bacterial Glycosyltransferases: Challenges and Opportunities of a Highly Diverse Enzyme Class Toward Tailoring Natural Products
title_full Bacterial Glycosyltransferases: Challenges and Opportunities of a Highly Diverse Enzyme Class Toward Tailoring Natural Products
title_fullStr Bacterial Glycosyltransferases: Challenges and Opportunities of a Highly Diverse Enzyme Class Toward Tailoring Natural Products
title_full_unstemmed Bacterial Glycosyltransferases: Challenges and Opportunities of a Highly Diverse Enzyme Class Toward Tailoring Natural Products
title_short Bacterial Glycosyltransferases: Challenges and Opportunities of a Highly Diverse Enzyme Class Toward Tailoring Natural Products
title_sort bacterial glycosyltransferases: challenges and opportunities of a highly diverse enzyme class toward tailoring natural products
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4757703/
https://www.ncbi.nlm.nih.gov/pubmed/26925049
http://dx.doi.org/10.3389/fmicb.2016.00182
work_keys_str_mv AT schmidjochen bacterialglycosyltransferaseschallengesandopportunitiesofahighlydiverseenzymeclasstowardtailoringnaturalproducts
AT heiderdominik bacterialglycosyltransferaseschallengesandopportunitiesofahighlydiverseenzymeclasstowardtailoringnaturalproducts
AT wendelnormaj bacterialglycosyltransferaseschallengesandopportunitiesofahighlydiverseenzymeclasstowardtailoringnaturalproducts
AT sperlnadine bacterialglycosyltransferaseschallengesandopportunitiesofahighlydiverseenzymeclasstowardtailoringnaturalproducts
AT siebervolker bacterialglycosyltransferaseschallengesandopportunitiesofahighlydiverseenzymeclasstowardtailoringnaturalproducts