Issue 17, 2011
From the journal:

Organic & Biomolecular Chemistry

A potential fortuitous binding of inhibitors of an inverting family GH9 β-glycosidase derived from isofagomine†

Solange Moréra,*a   Armelle Vigourouxa  and  Keith A. Stubbs*b  

* Corresponding authors

a Laboratoire d'Enzymologie et Biochimie Structurales (LEBS), CNRS, Avenue de la Terrasse, Gif-sur-Yvette, France
E-mail: morera@lebs.cnrs-gif.fr
Tel: +33 1 69823470

b Chemistry M313, School of Biomedical, Biomolecular and Chemical Sciences, The University of Western Australia, 35 Stirling Highway, Crawley, WA, Australia
E-mail: kstubbs@cyllene.uwa.edu.au
Tel: +61 8 6488 2725

Abstract

Using structural insight, the binding mode of isofagomine-derived inhibitors with family GH9 glycosidases is achieved via the study of Alicyclobacillus acidocaldarius (AaCel9A) endoglucanase. In contrast to what was observed in the first report using these compounds with inverting glycosidases from family GH6, these inhibitors do not adopt a distorted conformation in the active site.

Graphical abstract: A potential fortuitous binding of inhibitors of an inverting family GH9 β-glycosidase derived from isofagomine

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Article information

DOI
https://doi.org/10.1039/C1OB05766A
Article type
Communication
Submitted
16 May 2011
Accepted
07 Jun 2011
First published
25 Jul 2011

Org. Biomol. Chem., 2011,9, 5945-5947

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A potential fortuitous binding of inhibitors of an inverting family GH9 β-glycosidase derived from isofagomine

S. Moréra, A. Vigouroux and K. A. Stubbs, Org. Biomol. Chem., 2011, 9, 5945 DOI: 10.1039/C1OB05766A

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