@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.} }