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The Structural Basis of Glycosidase Inhibition by Five‐Membered Iminocyclitols: The Clan A Glycoside Hydrolase Endoglycoceramidase as a Model System
Author(s) -
Caines Matthew E. C.,
Hancock Susan M.,
Tarling Chris A.,
Wrodnigg Tanja M.,
Stick Robert V.,
Stütz Arnold E.,
Vasella Andrea,
Withers Stephen G.,
Strynadka Natalie C. J.
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200700268
Subject(s) - glycoside hydrolase , hydrolase , stereochemistry , chemistry , glycosyl , clan , glycoside , enzyme , computational biology , computer science , biochemistry , biology , sociology , anthropology
Fitting five into six : The crystal structure of a glycosidase‐bound, five‐membered iminocyclitol inhibitor was determined (see picture), and its binding interactions were compared to those of the classical six‐membered iminocyclitol inhibitors isofagomine and glucoimidazole and of the glycosyl–enzyme intermediate. This information may be used to develop more potent and specific therapeutically useful glycosidase inhibitors.