In order to accelerate the hydrolysis of glycosidic bonds by factors approaching 1017-fold, glycosidases have evolved finely tuned active sites optimally configured for transition-state stabilization. Structural analyses of various enzyme complexes representing stable intermediates along the reaction coordinate, in conjunction with detailed mechanistic studies on wild-type and mutant enzymes, have delineated the contributions of nucleophilic and general acid/base catalysis, as well as the roles of noncovalent interactions, to these impressive rate enhancements.
CITATION STYLE
Zechel, D. L., & Withers, S. G. (2000). Glycosidase mechanisms: Anatomy of a finely tuned catalyst. Accounts of Chemical Research, 33(1), 11–18. https://doi.org/10.1021/ar970172+
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