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Issue 21, 2006
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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

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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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Publication details

The article was received on 03 Jul 2006, accepted on 06 Sep 2006 and first published on 21 Sep 2006


Article type: Paper
DOI: 10.1039/B609455D
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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