ArticleBioconjugate chemistry2013
Use of novel mutant galactosyltransferase for the bioconjugation of terminal N-acetylglucosamine (GlcNAc) residues on live cell surface.
Article in Bioconjugate chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- A Time-Resolved FRET Assay Identifies a Small Molecule that Inhibits the Essential Bacterial Cell Wall Polymerase FtsW.Angewandte Chemie (International ed. in English) · 2023Article
- [Comparison of the performance of secretome analysis based on metabolic labeling by three unnatural sugars].Se pu = Chinese journal of chromatography · 2021Article
- Aberration of Serum and Tissue N-Glycans in Mouse β1,4-GalT1 Y286L Mutant Variants.Glycoconjugate journal · 2020Article
- Paramagnetic Tag for Glycosylation Sites in Glycoproteins: Structural Constraints on Heparan Sulfate Binding to Robo1.ACS chemical biology · 2018Article
- One-Step Selective Exoenzymatic Labeling (SEEL) Strategy for the Biotinylation and Identification of Glycoproteins of Living Cells.Journal of the American Chemical Society · 2016Article
- Glycosyltransferase engineering for carbohydrate synthesis.Biochemical Society transactions · 2016Review
- The challenge and promise of glycomics.Chemistry & biology · 2014Review
- Selective exo-enzymatic labeling of N-glycans on the surface of living cells by recombinant ST6Gal I.Angewandte Chemie (International ed. in English) · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
On the basis of the crystal structure of bovine β4Gal-T1 enzyme, mutation of a single amino acid Y289 to L289 (Y289L) changed its donor specificity from Gal to N-acetyl-galactosamine (GalNAc). A chemoenzymatic method that uses GalNAc analogues like GalNAz or 2-keto-Gal as sugar donors with the enzyme Y289L-β4Gal-T1 has identified hundreds of cytosolic and nuclear proteins that have O-GlcNAc modifications. To avoid potential cytotoxicity at Mn(2+) concentrations required to selectively modify GlcNAc residues on the surface of live cells, we have engineered a Mg(2+)-dependent enzyme. Previously, we found that the mutation of the metal-binding residue Met-344 to His-344 in bovine β4Gal-T1 enzyme altered its metal-ion specificity in such a way that the M344H-β4Gal-T1 enzyme exhibits better catalytic activity with Mg(2+) than with Mn(2+). Here, we find that, when these two mutations are combined, the double mutant, Y289L-M344H-β4Gal-T1, transfers GalNAc and its analogue sugars to the acceptor GlcNAc in the presence of Mg(2+). Using this mutant enzyme, we have detected free GlcNAc residues on the surface glycans of live HeLa cells and platelets. The specific transfer of a synthetic sugar with a chemical handle to the terminal GlcNAc residues on the surface of live cells provides a novel tool for selective modification, detection, and isolation of GlcNAc-ending glycans present on the cellular surface.
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