@article { ISI:000076481900008,
	title = {Bromoketone C-glycosides, a new class of beta-glucanase inactivators},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {120},
	number = {40},
	year = {1998},
	month = {OCT 14},
	pages = {10326-10331},
	abstract = {Although reliable methods have been developed for the labeling of the active site nucleophiles in glycosidases, no such reliable method has been developed for the identification of the acid/base catalyst. To address this problem two novel bromoketone affinity labels based on a beta-C-glucoside (6), and a beta-C-cellobioside (9), have been synthesized via a chemoenzymatic process and tested as inactivators of the beta-glucosidase from Agrobacterium sp. and the beta-glucanases from Cellulomonas fimi. The beta-glucosidase was inactivated by 6 in a time-dependent manner according to kinetic parameters of k(i) = 0.01 min(-1) and K-I = 3.1 mM. Electrospray ionization mass spectrometric analysis revealed that multiple labeling of the enzyme had occurred. The beta-endoglucanases, CenA and CenD, were inactivated stoicheometrically by 9 according to kinetic parameters of k(i) = 0.0155 min(-1); K-I = 0.35 mM and k(i) = 0.01 min(-1); K-I = 6.0 mM, respectively. These should therefore prove to be valuable reagents for the labeling of glycosidases.},
	issn = {0002-7863},
	doi = {10.1021/ja981580r},
	author = {Howard, S and Withers, SG}
}
