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 language||English (US)|
|Number of pages||6|
|Journal||Organic and Biomolecular Chemistry|
|State||Published - 2006|
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Organic Chemistry