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

Org. Biomol. Chem.2006 Nov 7;4(21):3945-50. doi:10.1039/b609455d. Epub 2006 Sep 21

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Cloning of E. coli K-12 orf8 (wbbI) and over-expression of the corresponding enzyme as a maltose-binding fusion protein provided recombinant WbbI beta-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 alpha-D-gluco-configuration but it also possessed the ability to turn-over acceptor analogues.

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

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