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  • Title: Biochemical characterization of a glycosyltransferase homolog from an oral pathogen Fusobacterium nucleatum as a human glycan-modifying enzyme.
    Author: Kim S, Oh DB, Kwon O, Jung JG, Lee YM, Ko K, Ko JH, Kang HA.
    Journal: J Microbiol Biotechnol; 2008 May; 18(5):859-65. PubMed ID: 18633282.
    Abstract:
    Bacterial glycosyltransferases have drawn growing attention as economical enzymes for oligosaccharide synthesis, with their easy expression and relatively broad substrate specificity. Here, we characterized a glycosyltransferase homolog (Fnu_GT) from a human oral pathogen, Fusobacterium nucleatum. Bioinformatic analysis showed that Fnu_GT belongs to the glycosyltransferases family II. The recombinant Fnu_GT (rFnu_GT) expressed in Escherichia coli displayed the highest glycosylation activity when UDP-galactose (Gal) was used as a donor nucleotide-sugar with heptose or Nacetylglucosamine (GlcNAc) as an acceptor sugar. Interestingly, rFnu_GT transferred the galactose moiety of UDP-Gal to a nonreducing terminal GlcNAc attached to the trimannosyl core glycan, indicating its potential as an enzyme for humantype N-glycan synthesis.
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