Expression and initial characterization of WbbI, a putative d-Galf:α-d-Glc β-1,6-galactofuranosyltransferase from Escherichia coli K-12

Corin Wing, James C. Errey, Balaram Mukhopadhyay, John S. Blanchard, Robert A. Field

Research output: Contribution to journalArticle

32 Scopus citations


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 languageEnglish (US)
Pages (from-to)3945-3950
Number of pages6
JournalOrganic and Biomolecular Chemistry
Issue number21
Publication statusPublished - Oct 25 2006


ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

Cite this