Issue 21, 2006
From the journal:

Organic & Biomolecular Chemistry

Expression and initial characterization of WbbI, a putative d-Galf:α-d-Glc β-1,6-galactofuranosyltransferase from Escherichia coli K-12

Corin Wing,a   James C. Errey,b   Balaram Mukhopadhyay,a   John S. Blanchardb  and  Robert A. Field*a  

* Corresponding authors

a Centre for Carbohydrate Chemistry, School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich, U.K
E-mail: r.a.field@uea.ac.uk

b Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York, USA

Abstract

Cloning of E. coli K-12 orf8 (wbbI) and over-expression of the corresponding enzyme as a maltose-binding fusion protein provided recombinant WbbI β-1,6-galactofuranosyltransferase activity. Challenged with synthetic acceptor analogues in the presence of UDP-galactofuranose as a donor, WbbI showed a modest preference for pyranoside acceptor substrates of the α-D-gluco-configuration but it also possessed the ability to turn-over acceptor analogues.

Graphical abstract: Expression and initial characterization of WbbI, a putative d-Galf:α-d-Glc β-1,6-galactofuranosyltransferase from Escherichia coli K-12

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Article information

DOI
https://doi.org/10.1039/B609455D
Article type
Paper
Submitted
03 Jul 2006
Accepted
06 Sep 2006
First published
21 Sep 2006

Org. Biomol. Chem., 2006,4, 3945-3950

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Expression and initial characterization of WbbI, a putative D-Galf:α-D-Glc β-1,6-galactofuranosyltransferase from Escherichia coli K-12

C. Wing, J. C. Errey, B. Mukhopadhyay, J. S. Blanchard and R. A. Field, Org. Biomol. Chem., 2006, 4, 3945 DOI: 10.1039/B609455D

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