Issue 5, 2008
From the journal:

Organic & Biomolecular Chemistry

Probing the β-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants†

Victoria A. Money,a   Alan Cartmell,b   Catarina I. P. D. Guerreiro,c   Valerie M.-A. Ducros,a   Carlos M. G. A. Fontes,c   Harry J. Gilbertb  and  Gideon J. Davies*a  

* Corresponding authors

a Structural Biology Laboratory, Department of Chemistry, The University of York, Heslington, York, U.K.
E-mail: davies@ysbl.york.ac.uk
Fax: 44-1904-32826
Tel: 44-1904-328260

b Institute for Cell and Molecular Biosciences, Newcastle University, 2nd floor Catherine Cookson Building, The Medical School Framlington Place, Newcastle upon Tyne, U.K.

c CIISA-Faculdade de Medicina Veterinária, Universidade Técnica de Lisboa, Avenida da Universidade Técnica, 1300-477 Lisboa, Portugal

Abstract

The substrate binding regions of a β-1,3:1,4 glucanase are revealed through structural analysis with a thio-oligosaccharide and kinetics of enzyme variants.

Graphical abstract: Probing the β-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants

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Article information

DOI
https://doi.org/10.1039/B719288F
Article type
Communication
Submitted
13 Dec 2007
Accepted
10 Jan 2008
First published
04 Feb 2008

Org. Biomol. Chem., 2008,6, 851-853

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Probing the β-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants

V. A. Money, A. Cartmell, C. I. P. D. Guerreiro, V. M.-A. Ducros, C. M. G. A. Fontes, H. J. Gilbert and G. J. Davies, Org. Biomol. Chem., 2008, 6, 851 DOI: 10.1039/B719288F

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