Biochemical Characterization of a Glycosyltransferase Homolog from an Oral Pathogen Fusobacterium nucleatum as a Human Glycan-Modifying Enzyme

  • Kim, Seong-Hun (Omics and Integration Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Oh, Doo-Byoung (Omics and Integration Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Kwon, Oh-Suk (Omics and Integration Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Jung, Jae-Kap (Omics and Integration Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Lee, Yun-Mi (Omics and Integration Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Ko, Ki-Sung (Division of Biological Science, College of Natural Science, Wonkwang University) ;
  • Ko, Jeong-Heon (Omics and Integration Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Kang, Hyun-Ah (Omics and Integration Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
  • Published : 2008.05.31

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 N-acetylglucosamine (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 human-type N-glycan synthesis.

Keywords

References

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