@article { ISI:000084992000003,
	title = {Glycosidase mechanisms: Anatomy of a finely tuned catalyst},
	journal = {ACCOUNTS OF CHEMICAL RESEARCH},
	volume = {33},
	number = {1},
	year = {2000},
	month = {JAN},
	pages = {11-18},
	abstract = {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.},
	issn = {0001-4842},
	doi = {10.1021/ar970172+},
	author = {Zechel, DL and Withers, SG}
}
