Issue 8, 2003
From the journal:

Chemical Communications

A xylobiose-derived isofagomine lactam glycosidase inhibitor binds as its amide tautomer†

Tracey Gloster,a   Spencer J. Williams,b   Chris A. Tarling,c   Shirley Roberts,a   Claude Dupont,d   Pascale Jodoin,d   François Shareck,d   Stephen G. Withersc  and  Gideon J. Davies*a  

* Corresponding authors

a Structural Biology Laboratory, Department of Chemistry, The University of York, Heslington, UK
E-mail: davies@ysbl.york.ac.uk

b School of Chemistry, University of Melbourne, Parkville, Australia 3010
E-mail: sjwill@unimelb.edu.au

c Department of Chemistry, 2036 Main Mall, University of British Columbia, Vancouver, Canada V6T 1Z1
E-mail: withers@chem.ubc.ca

d Institut national de la recherche scientifique, INRS-Institut Armand-Frappier, 531 boul des Prairies, Laval, Québec, Canada, H7V 1B7
E-mail: Claude.Dupont@inrs-iaf.uquebec.ca

Abstract

The atomic-resolution structure of a xylobiose-derived isofagomine lactam in complex with the xylanase Xyn10A from Streptomyces lividans reveals that the lactam is bound to the enzyme as the amide tautomer, with “reversed” protonation-states for nucleophile and acid–base.

Graphical abstract: A xylobiose-derived isofagomine lactam glycosidase inhibitor binds as its amide tautomer

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Article information

DOI
https://doi.org/10.1039/B301829F
Article type
Communication
Submitted
17 Feb 2003
Accepted
05 Mar 2003
First published
20 Mar 2003

Chem. Commun., 2003, 944-945

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A xylobiose-derived isofagomine lactam glycosidase inhibitor binds as its amide tautomer

T. Gloster, S. J. Williams, C. A. Tarling, S. Roberts, C. Dupont, P. Jodoin, F. Shareck, S. G. Withers and G. J. Davies, Chem. Commun., 2003, 944 DOI: 10.1039/B301829F

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