Molecular Basis for Trehalase Inhibition Revealed by the Structure of Trehalase in Complex with Potent Inhibitors

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) rev...

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Published inAngewandte Chemie International Edition Vol. 46; no. 22; pp. 4115 - 4119
Main Authors Gibson, Robert P., Gloster, Tracey M., Roberts, Shirley, Warren, R. Anthony J., Storch de Gracia, Isabel, García, Ángela, Chiara, Jose L., Davies, Gideon J.
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 01.01.2007
WILEY‐VCH Verlag
Subjects
Catalysis
Colorimetry
Disaccharides - antagonists & inhibitors
Disaccharides - chemistry
Enzyme Inhibitors - pharmacology
Hydrogen Bonding
inhibitors
Inositol - analogs & derivatives
Inositol - antagonists & inhibitors
Inositol - chemistry
Protein Conformation
protein structures
Trehalase - antagonists & inhibitors
Trehalase - chemistry
trehalases
trehazolins
validoxylamines
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Summary: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.
Bibliography:R.P.G. and T.M.G. contributed equally to this work. This work was funded by the Biotechnology and Biological Sciences Research Council (BBSRC). G.J.D. holds a Royal Society Wolfson Merit Award. The authors thank Anthony O'Sullivan (Syngenta) for the provision of compound 2 and for useful discussions.
Royal Society
istex:D9AEE3B549968D660A726ED4F2AB3DC943C6A390
ArticleID:ANIE200604825
ark:/67375/WNG-2BN0XR6G-4
Biotechnology and Biological Sciences Research Council (BBSRC)
R.P.G. and T.M.G. contributed equally to this work. This work was funded by the Biotechnology and Biological Sciences Research Council (BBSRC). G.J.D. holds a Royal Society Wolfson Merit Award. The authors thank Anthony O'Sullivan (Syngenta) for the provision of compound
and for useful discussions.
2
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ObjectType-Feature-2
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ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200604825