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Author(s) -
Fort Sébastien,
Varrot Annabelle,
Schülein Martin,
Cottaz Sylvain,
Driguez Hugues,
Davies Gideon J.
Publication year - 2001
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20010504)2:5<297::aid-cbic297>3.0.co;2-6
Subject(s) - glycoside hydrolase , hydrolase , active site , chemistry , stereochemistry , linkage (software) , biochemistry , enzyme , gene
The cover picture shows the “wire‐cage” representation of the electron density (drawn in red) for a novel glycosidase inhibitor bound in the active site of a glycoside hydrolase, endoglucanase Cel5A from Bacillus agaradhaerens. These compounds incorporate an α ‐ D ‐sugar in an otherwise all‐ β ‐ D ‐oligosaccharide. This counterintuitive geometric feature allows the inhibitors to span the active centre of a retaining glycoside hydrolase, utilising binding energy from many subsites without the need for substrate distortion. A schematic representation of the mode of binding of the mixed‐linkage inhibitor is shown in the top left corner. More about these new compounds that open up the possibility for developing new strategies for glycosidase inhibition can be found in the paper by G. J. Davies et al. on p. 319 ff.