|Title||Glycosidase mechanisms: Anatomy of a finely tuned catalyst|
|Publication Type||Journal Article|
|Year of Publication||2000|
|Authors||Zechel, DL, Withers, SG|
|Journal||ACCOUNTS OF CHEMICAL RESEARCH|
In order to accelerate the hydrolysis of glycosidic bonds by factors approaching 10(17)-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.