Glycosidase mechanisms: anatomy of a finely tuned catalyst.
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.
Zechel
D L
DL
Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada.
Withers
S G
SG
D002384:Catalysis; D018360:Crystallography, X-Ray; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D016296:Mutagenesis; D011487:Protein Conformation; D013379:Substrate Specificity
D006026:Glycoside Hydrolases