@article { ISI:000075614600018,
	title = {Insights into transition state stabilization of the beta-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants},
	journal = {NATURE STRUCTURAL BIOLOGY},
	volume = {5},
	number = {9},
	year = {1998},
	month = {SEP},
	pages = {812-818},
	abstract = {The catalytic mechanism of {\textquoteleft}retaining{\textquoteright} beta-glycosidases has been the subject of considerable interest and debate for many years. The visualization of a covalent glycosyl enzyme intermediate by X-ray crystallography was first accomplished with a saccharide substrate substituted with fluorine at its 2-position. The structure implicated major roles for residue His 205 and for the a-hydroxyl position of the proximal saccharide in binding and catalysis. Here we have studied the kinetic behavior of various His 205 mutants. One of these mutants, a double mutant H205N/E127A, has been used to stabilize a covalent glycosyl-enzyme intermediate involving an unsubstituted sugar, permitting crystallographic analysis of the interactions between its 2-hydroxyl group and the enzyme.},
	issn = {1072-8368},
	doi = {10.1038/1852},
	author = {Notenboom, V and Birsan, C and Nitz, M and ROSE, DR and WARREN, RAJ and Withers, SG}
}
