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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacteria / classification
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Bacteria / enzymology
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Bacteria / genetics
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism
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Cloning, Molecular
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Enzyme Stability
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Fusobacterium nucleatum / chemistry
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Fusobacterium nucleatum / enzymology*
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Fusobacterium nucleatum / genetics
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Gene Expression
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Glycosyltransferases / chemistry*
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Glycosyltransferases / genetics
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Glycosyltransferases / isolation & purification
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Glycosyltransferases / metabolism
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Humans
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Hydrolysis
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Kinetics
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Molecular Sequence Data
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Mouth / microbiology*
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Phylogeny
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Polysaccharides / metabolism*
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Sequence Homology, Amino Acid
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Substrate Specificity
Substances
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Bacterial Proteins
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Polysaccharides
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Glycosyltransferases