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 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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Chromatography, Thin Layer
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Escherichia coli / enzymology*
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Escherichia coli Proteins / isolation & purification
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Escherichia coli Proteins / metabolism*
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Glycosyltransferases / isolation & purification
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Glycosyltransferases / metabolism*
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Oligosaccharides / chemistry
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Fusion Proteins / metabolism
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Substrate Specificity
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Time Factors
Substances
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Escherichia coli Proteins
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Oligosaccharides
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Recombinant Fusion Proteins
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Glycosyltransferases
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wbbI protein, E coli