期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 28, 期 -, 页码 1-13出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2014.06.003
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资金
- Australian Research Council (ARC)
- University of Melbourne
- ARC
- Biotechnology and Biological Sciences Research Council
- European Research Council
Glycoside hydrolases (GHs) are classified into >100 sequencebased 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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