Biochemical charactrization of a glycosyltransferase homolog from an oral pathogen Fusobacterium nucleatum as a human glycan-modifying enzyme

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Title
Biochemical charactrization of a glycosyltransferase homolog from an oral pathogen Fusobacterium nucleatum as a human glycan-modifying enzyme
Author(s)
Seong Hun KimDoo-Byoung OhOh Suk Kwon; J K Jeong; Yun Mi Lee; K Ko; Jeong Heon Ko; H A Kang
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 18, no. 5, pp. 859-865
Publication Year
2008
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
Keyword
Glycosyltransferasenucleotide-sugarFusobacterium nucleatumhuman-type N-linked glycan
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
Aging Convergence Research Center > 1. Journal Articles
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
Synthetic Biology and Bioengineering Research Institute > Genome Editing Research Center > 1. Journal Articles
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