Expression and initial characterization of WbbI, a putative D-Galf:alpha-D-Glc beta-1,6-galactofuranosyltransferase from Escherichia coli K-12.
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.
Wing
Corin
C
Centre for Carbohydrate Chemistry, School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich, NR4 7TJ, UK.
Errey
James C
JC
Mukhopadhyay
Balaram
B
Blanchard
John S
JS
Field
Robert A
RA
D002855:Chromatography, Thin Layer; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000302:isolation & purification / Q000378:metabolism*; D016695:Glycosyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D009844:Oligosaccharides / Q000737:chemistry; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity; D013997:Time Factors
D029968:Escherichia coli Proteins; D009844:Oligosaccharides; D011993:Recombinant Fusion Proteins; D016695:Glycosyltransferases; C522196:wbbI protein, E coli