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Dissecting conformational contributions to glycosidase catalysis and inhibition

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JournalCURRENT OPINION IN STRUCTURAL BIOLOGY
DateE-pub ahead of print - 10 Jul 2014
DatePublished (current) - Oct 2014
Issue number1
Volume28
Number of pages13
Pages (from-to)1-13
Early online date10/07/14
Original languageEnglish

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.

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© 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/).

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