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A mechanism of glucose tolerance and stimulation of GH1 β-glucosidases

β-Glucosidases are enzymes that hydrolyze β-glycosidic bonds to release non-reducing terminal glucosyl residues from glycosides and oligosaccharides, and thus have significant application potential in industries. However, most β-glucosidases are feedback inhibited by the glucose product, which restr...

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Autores principales: Yang, Yang, Zhang, Xinxin, Yin, Qiang, Fang, Wei, Fang, Zemin, Wang, Xiaotang, Zhang, Xuecheng, Xiao, Yazhong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4658561/
https://www.ncbi.nlm.nih.gov/pubmed/26603650
http://dx.doi.org/10.1038/srep17296
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author Yang, Yang
Zhang, Xinxin
Yin, Qiang
Fang, Wei
Fang, Zemin
Wang, Xiaotang
Zhang, Xuecheng
Xiao, Yazhong
author_facet Yang, Yang
Zhang, Xinxin
Yin, Qiang
Fang, Wei
Fang, Zemin
Wang, Xiaotang
Zhang, Xuecheng
Xiao, Yazhong
author_sort Yang, Yang
collection PubMed
description β-Glucosidases are enzymes that hydrolyze β-glycosidic bonds to release non-reducing terminal glucosyl residues from glycosides and oligosaccharides, and thus have significant application potential in industries. However, most β-glucosidases are feedback inhibited by the glucose product, which restricts their application. Remarkably, some β-glucosidases of the glycoside hydrolase (GH) 1 family are tolerant to or even stimulated by glucose. Elucidation of the mechanisms of glucose tolerance and stimulation of the GH1 β-glucosidases will be crucial to improve their application through enzyme engineering. In this study, by comparing the primary and tertiary structures of two GH1 β-glucosidases with distinct glucose dependence, some putative glucose-dependence relevant sites were mutated to investigate their exact roles. Both biochemical and structural characterization of the mutants suggested that some sites at the entrance and middle of the substrate channel regulate the effects of glucose, and the relative binding affinity/preference of these sites to glucose modulates the glucose dependence. A mechanism was therefore proposed to interpret the glucose dependence of GH1 β-glucosidases. This research provides fresh insight into our current understanding of the properties and mechanisms of GH1 β-glycosidases and related enzymes that modulate their activity via feedback control mechanism.
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spelling pubmed-46585612015-11-30 A mechanism of glucose tolerance and stimulation of GH1 β-glucosidases Yang, Yang Zhang, Xinxin Yin, Qiang Fang, Wei Fang, Zemin Wang, Xiaotang Zhang, Xuecheng Xiao, Yazhong Sci Rep Article β-Glucosidases are enzymes that hydrolyze β-glycosidic bonds to release non-reducing terminal glucosyl residues from glycosides and oligosaccharides, and thus have significant application potential in industries. However, most β-glucosidases are feedback inhibited by the glucose product, which restricts their application. Remarkably, some β-glucosidases of the glycoside hydrolase (GH) 1 family are tolerant to or even stimulated by glucose. Elucidation of the mechanisms of glucose tolerance and stimulation of the GH1 β-glucosidases will be crucial to improve their application through enzyme engineering. In this study, by comparing the primary and tertiary structures of two GH1 β-glucosidases with distinct glucose dependence, some putative glucose-dependence relevant sites were mutated to investigate their exact roles. Both biochemical and structural characterization of the mutants suggested that some sites at the entrance and middle of the substrate channel regulate the effects of glucose, and the relative binding affinity/preference of these sites to glucose modulates the glucose dependence. A mechanism was therefore proposed to interpret the glucose dependence of GH1 β-glucosidases. This research provides fresh insight into our current understanding of the properties and mechanisms of GH1 β-glycosidases and related enzymes that modulate their activity via feedback control mechanism. Nature Publishing Group 2015-11-25 /pmc/articles/PMC4658561/ /pubmed/26603650 http://dx.doi.org/10.1038/srep17296 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Yang, Yang
Zhang, Xinxin
Yin, Qiang
Fang, Wei
Fang, Zemin
Wang, Xiaotang
Zhang, Xuecheng
Xiao, Yazhong
A mechanism of glucose tolerance and stimulation of GH1 β-glucosidases
title A mechanism of glucose tolerance and stimulation of GH1 β-glucosidases
title_full A mechanism of glucose tolerance and stimulation of GH1 β-glucosidases
title_fullStr A mechanism of glucose tolerance and stimulation of GH1 β-glucosidases
title_full_unstemmed A mechanism of glucose tolerance and stimulation of GH1 β-glucosidases
title_short A mechanism of glucose tolerance and stimulation of GH1 β-glucosidases
title_sort mechanism of glucose tolerance and stimulation of gh1 β-glucosidases
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4658561/
https://www.ncbi.nlm.nih.gov/pubmed/26603650
http://dx.doi.org/10.1038/srep17296
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