ArticleScientific reports2016
A rationally engineered yeast pyruvyltransferase Pvg1p introduces sialylation-like properties in neo-human-type complex oligosaccharide.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Bacillus subtilis EpsA-O: A novel exopolysaccharide structure acting as an efficient adhesive in biofilms.NPJ biofilms and microbiomes · 2024Article
- Molecular modelling and site-directed mutagenesis provide insight into saccharide pyruvylation by the Paenibacillus alvei CsaB enzyme.Scientific reports · 2023Article
- Identification of a second glycoform of the clinically prevalent O1 antigen fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- AssayingBiomolecules · 2021Article
- A cell-free biosynthesis platform for modular construction of protein glycosylation pathways.Nature communications · 2019Article
- Pyruvate Substitutions on Glycoconjugates.International journal of molecular sciences · 2019Review
- Draft Genome Sequence of Bacillus sp. HMA207, a Strain That Exhibits β-d-Galactosidase Activity To Release Pyruvylated Galactose.Microbiology resource announcements · 2018Article
- Identification and characterization of a novel β-D-galactosidase that releases pyruvylated galactose.Scientific reports · 2018Article
- Functional Characterization of Enzymatic Steps Involved in Pyruvylation of Bacterial Secondary Cell Wall Polymer Fragments.Frontiers in microbiology · 2018Article
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9 authors.
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Abstract
Pyruvylation onto the terminus of oligosaccharide, widely seen from prokaryote to eukaryote, confers negative charges on the cell surface and seems to be functionally similar to sialylation, which is found at the end of human-type complex oligosaccharide. However, detailed molecular mechanisms underlying pyruvylation have not been clarified well. Here, we first determined the crystal structure of fission yeast pyruvyltransferase Pvg1p at a resolution of 2.46 Å. Subsequently, by combining molecular modeling with mutational analysis of active site residues, we obtained a Pvg1p mutant (Pvg1p(H168C)) that efficiently transferred pyruvyl moiety onto a human-type complex glycopeptide. The resultant pyruvylated human-type complex glycopeptide recognized similar lectins on lectin arrays as the α2,6-sialyl glycopeptides. This newly-generated pyruvylation of human-type complex oligosaccharides would provide a novel method for glyco-bioengineering.
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