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Molecular Basis for Trehalase Inhibition Revealed by the Structure of Trehalase in Complex with Potent Inhibitors
Author(s) -
Gibson Robert P.,
Gloster Tracey M.,
Roberts Shirley,
Warren R. Anthony J.,
Storch de Gracia Isabel,
García Ángela,
Chiara Jose L.,
Davies Gideon 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.200604825
Subject(s) - trehalase , disaccharide , chemistry , trehalose , enzyme , hydrolysis , biochemistry , stereochemistry , hydrogen bond , glycoside hydrolase , molecule , organic chemistry
Strong inhibitions : The inhibition of trehalases, enzymes which hydrolyze the disaccharide trehalose, is a target for novel antibiotic insecticides. The structures (see picture; C black, N blue, O red, S yellow) of a trehalase in complex with validoxylamine A (yellow) and 1‐thiatetrazolin (blue) reveal that the inhibitors tightly bind to the enzyme through hydrogen bonds.

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