Speciale, Gaetono, Thompson, Andrew James orcid.org/0000-0001-7865-1856, Davies, Gideon John orcid.org/0000-0002-7343-776X et al. (1 more author) (2014) Dissecting conformational contributions to glycosidase catalysis and inhibition. CURRENT OPINION IN STRUCTURAL BIOLOGY. pp. 1-13. ISSN 0959-440X
Abstract
Glycoside hydrolases (GHs) are classified into >100 sequence-based families. These enzymes process a wide variety of complex carbohydrates with varying stereochemistry at the anomeric and other ring positions. The shapes that these sugars adopt upon binding to their cognate GHs, and the conformational changes that occur along the catalysis reaction coordinate is termed the conformational itinerary. Efforts to define the conformational itineraries of GHs have focussed upon the critical points of the reaction: substrate-bound (Michaelis), transition state, intermediate (if relevant) and product-bound. Recent approaches to defining conformational itineraries that marry X-ray crystallography of enzymes bound to ligands that mimic the critical points, along with advanced computational methods and kinetic isotope effects are discussed.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2014 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/3.0/). |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Funding Information: | Funder Grant number BBSRC (BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL) BB/G016127/1 |
Depositing User: | Pure (York) |
Date Deposited: | 17 Mar 2015 17:43 |
Last Modified: | 16 Oct 2024 12:24 |
Published Version: | https://doi.org/10.1016/j.sbi.2014.06.003 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1016/j.sbi.2014.06.003 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:84289 |
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Description: Dissecting conformational contributions to glycosidase catalysis and inhibition