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, R.A. Field

Research output: Contribution to journalArticlepeer-review


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.
Original languageUndefined
Pages (from-to)3945-3950
Number of pages6
JournalOrganic and Biomolecular Chemistry
Issue number21
Publication statusPublished - 2006


  • Cloning
  • Conformations
  • Enzymes
  • Escherichia coli
  • Maltose

Research Beacons, Institutes and Platforms

  • Manchester Institute of Biotechnology

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