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Elsevier, Current Opinion in Structural Biology, (28), p. 1-13, 2014

DOI: 10.1016/j.sbi.2014.06.003

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Dissecting conformational contributions to glycosidase catalysis and inhibition

Journal article published in 2014 by Gaetano Speciale ORCID, Andrew James Thompson ORCID, Gideon John Davies ORCID, Spencer J. Williams ORCID
This paper is available in a repository.
This paper is available in a repository.

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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.