ArticleBioorganic & medicinal chemistry2016
Donor substrate promiscuity of bacterial β1-3-N-acetylglucosaminyltransferases and acceptor substrate flexibility of β1-4-galactosyltransferases.
Article in Bioorganic & medicinal chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 65 citations in OpenAlex.
- Advances in chemoenzymatic synthesis of glycosaminoglycans and proteoglycans.Current opinion in chemical biology · 2026Review
- Defining substrate specificities ofOrganic chemistry frontiers : an international journal of organic chemistry · 2026Article
- Divergent Enzymatic Synthesis of a Comprehensive Type‑1 Glycan Determinant Library.ACS catalysis · 2025Article
- Glycan synthesis with SpyCatcher-SpyTag immobilized Leloir-glycosyltransferases.Applied microbiology and biotechnology · 2025Article
- Chemoenzymatic Synthesis of Glycosphingolipids Having an HNK-1 Epitope for Erythrocyte Cell Surface Remodeling.Journal of the American Chemical Society · 2025Article
- Orthogonal-Group-Controlled Site-Selective I-Branching of Poly-N-acetyllactosamine Chains Reveals Unique Binding Specificities of Proteins towards I-Antigens.Angewandte Chemie (International ed. in English) · 2025Article
- Chemoenzymatic Synthesis of Keratan Sulfate Oligosaccharides Using UDP-Galactose-6-aldehyde To Control Sulfation at Galactosides.Organic letters · 2024Article
- A bifunctionalOrganic & biomolecular chemistry · 2024Article
- Engineered plants provide a photosynthetic platform for the production of diverse human milk oligosaccharides.Nature food · 2024Article
- A Biomimetic Synthetic Strategy Can Provide Keratan Sulfate I and II Oligosaccharides with Diverse Fucosylation and Sulfation Patterns.Journal of the American Chemical Society · 2024Article
- Exploiting Substrate Specificities of 6-JACS Au · 2023Article
- Glycoprotein In Vitro N-Glycan Processing Using Enzymes Expressed inMolecules (Basel, Switzerland) · 2023Article
- Digital microfluidics-engaged automated enzymatic degradation and synthesis of oligosaccharides.Frontiers in bioengineering and biotechnology · 2023Article
- Substrate and Process Engineering for Biocatalytic Synthesis and Facile Purification of Human Milk Oligosaccharides.ChemSusChem · 2022Article
- Enzymatic Synthesis of Glycans and Glycoconjugates.Advances in biochemical engineering/biotechnology · 2021Review
- Machine-Driven Chemoenzymatic Synthesis of Glycopeptide.Angewandte Chemie (International ed. in English) · 2020Article
- EngineerACS catalysis · 2020Article
- A Bacterial β1-3-Galactosyltransferase Enables Multigram-Scale Synthesis of Human Milk Lacto-ACS catalysis · 2019Article
- A cell-free biosynthesis platform for modular construction of protein glycosylation pathways.Nature communications · 2019Article
- Enzymatic Cascades for TailoredMolecules (Basel, Switzerland) · 2019Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
β1-3-N-Acetylglucosaminyltransferases (β3GlcNAcTs) and β1-4-galactosyltransferases (β4GalTs) have been broadly used in enzymatic synthesis of N-acetyllactosamine (LacNAc)-containing oligosaccharides and glycoconjugates including poly-LacNAc, and lacto-N-neotetraose (LNnT) found in the milk of human and other mammals. In order to explore oligosaccharides and derivatives that can be synthesized by the combination of β3GlcNAcTs and β4GalTs, donor substrate specificity studies of two bacterial β3GlcNAcTs from Helicobacter pylori (Hpβ3GlcNAcT) and Neisseria meningitidis (NmLgtA), respectively, using a library of 39 sugar nucleotides were carried out. The two β3GlcNAcTs have complementary donor substrate promiscuity and 13 different trisaccharides were produced. They were used to investigate the acceptor substrate specificities of three β4GalTs from Neisseria meningitidis (NmLgtB), Helicobacter pylori (Hpβ4GalT), and bovine (Bβ4GalT), respectively. Ten of the 13 trisaccharides were shown to be tolerable acceptors for at least one of these β4GalTs. The application of NmLgtA in one-pot multienzyme (OPME) synthesis of two trisaccharides including GalNAcβ1-3Galβ1-4GlcβProN3 and Galβ1-3Galβ1-4Glc was demonstrated. The study provides important information for using these glycosyltransferases as powerful catalysts in enzymatic and chemoenzymatic syntheses of oligosaccharides and derivatives which can be useful probes and reagents.
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