@article { ISI:000375008700012,
	title = {Glucosyl epi-cyclophellitol allows mechanism-based inactivation and structural analysis of human pancreatic alpha-amylase},
	journal = {FEBS LETTERS},
	volume = {590},
	number = {8},
	year = {2016},
	month = {APR},
	pages = {1143-1151},
	abstract = {As part of a search for selective, mechanism-based covalent inhibitors of human pancreatic alpha-amylase we describe the chemoenzymatic synthesis of the disaccharide analog alpha-glucosyl epi-cyclophellitol, demonstrate its stoichiometric reaction with human pancreatic alpha-amylase and evaluate the time dependence of its inhibition. X-ray crystallographic analysis of the covalent derivative so formed confirms its reaction at the active site with formation of a covalent bond to the catalytic nucleophile D197. The structure illuminates the interactions with the active site and confirms OH4{\textquoteright} on the nonreducing end sugar as a good site for attachment of fluorescent tags in generating probes for localization and quantitation of amylase in vivo.},
	issn = {0014-5793},
	doi = {10.1002/1873-3468.12143},
	author = {Caner, Sami and Zhang, Xiaohua and Jiang, Jianbing and Chen, Hong-Ming and Nguyen, Nham T. and Overkleeft, Hermen and Brayer, Gary D. and Withers, Stephen G.}
}
