@article { ISI:A1995TD84500033,
	title = {SUBSTRATE-INDUCED INACTIVATION OF A CRIPPLED BETA-GLUCOSIDASE MUTANT - IDENTIFICATION OF THE LABELED AMINO-ACID AND MUTAGENIC ANALYSIS OF ITS ROLE},
	journal = {BIOCHEMISTRY},
	volume = {34},
	number = {44},
	year = {1995},
	month = {NOV 7},
	pages = {14547-14553},
	abstract = {The beta-glucosidase from Agrobacterium sp. catalyzes the hydrolysis of beta-glucosides via a covalent alpha-D-glucopyranosyl-enzyme intermediate involving Glu358. Hydrolysis of 2,4-dinitrophenyl beta-D-glucopyranoside by the low activity Glu358Asp mutant of Agrobacterium beta-glucosidase is accompanied by time-dependent inactivation of the enzyme. Through kinetic studies, labeling, and sequence analysis, inactivation is shown to be a consequence of the occasional (1 time in 1100) attack of Tyr298 on the anomeric center of the substrate, in place of the catalytic nucleophile, with formation of a stable alpha-D-glucopyranosyl tyrosine residue. Tyr298 is conserved throughout family 1 of glycoside hydrolases, an indication of a possible role in catalysis. Results of a kinetic analysis of the Tyr298Phe mutant are consistent with a function of Tyr298 in both orienting the nearby nucleophile Glu358 and stabilizing its deprotonated state in the free enzyme.},
	issn = {0006-2960},
	doi = {10.1021/bi00044a033},
	author = {GEBLER, JC and TRIMBUR, DE and WARREN, AJ and AEBERSOLD, R and NAMCHUK, M and Withers, SG}
}
