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 Citations (Scopus)

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 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
Volume4
Issue number21
DOIs
StatePublished - 2006

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Maltose-Binding Proteins
Recombinant Fusion Proteins
Maltose
Cloning
Escherichia
Escherichia coli
Organism Cloning
analogs
Substrates
Enzymes
enzymes
fusion
proteins
configurations
uridine diphosphate galactofuranose

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Chemistry(all)

Cite this

Expression and initial characterization of WbbI, a putative d-Galf : α-d-Glc β-1,6-galactofuranosyltransferase from Escherichia coli K-12. / Wing, Corin; Errey, James C.; Mukhopadhyay, Balaram; Blanchard, John S.; Field, Robert A.

In: Organic and Biomolecular Chemistry, Vol. 4, No. 21, 2006, p. 3945-3950.

Research output: Contribution to journalArticle

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