ArticleMolecular bioSystems2011
Decreasing the sialidase activity of multifunctional Pasteurella multocida α2-3-sialyltransferase 1 (PmST1) by site-directed mutagenesis.
Article in Molecular bioSystems, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Determinants of undesired α2-6-sialoside formation by PmST1 M144D.Organic & biomolecular chemistry · 2026Article
- Enabling Chemoenzymatic Strategies and Enzymes for Synthesizing Sialyl Glycans and Sialyl Glycoconjugates.Accounts of chemical research · 2024Article
- Systematic synthesis of bisectedChemical science · 2022Article
- One-pot multienzyme (OPME) chemoenzymatic synthesis of brain ganglioside glycans with human ST3GAL II expressed inChemCatChem · 2022Article
- Cellular and Molecular Engineering of Glycan Sialylation in Heterologous Systems.Molecules (Basel, Switzerland) · 2021Review
- Facile Chemoenzymatic Synthesis of O-Mannosyl Glycans.Angewandte Chemie (International ed. in English) · 2018Article
- Streamlined chemoenzymatic total synthesis of prioritized ganglioside cancer antigens.Organic & biomolecular chemistry · 2018Article
- α2-6-Neosialidase: A Sialyltransferase Mutant as a Sialyl Linkage-Specific Sialidase.ACS chemical biology · 2018Article
- Converting Pasteurella multocidaα2-3-sialyltransferase 1 (PmST1) to a regioselective α2-6-sialyltransferase by saturation mutagenesis and regioselective screening.Organic & biomolecular chemistry · 2017Article
- Identification of the binding roles of terminal and internal glycan epitopes using enzymatically synthesized N-glycans containing tandem epitopes.Organic & biomolecular chemistry · 2016Article
- Overcoming the limited availability of human milk oligosaccharides: challenges and opportunities for research and application.Nutrition reviews · 2016Review
- Substrate specificity of FUT8 and chemoenzymatic synthesis of core-fucosylated asymmetric N-glycans.Organic & biomolecular chemistry · 2016Article
- One-pot multienzyme (OPME) systems for chemoenzymatic synthesis of carbohydrates.Organic & biomolecular chemistry · 2016Article
- Glycosyltransferase engineering for carbohydrate synthesis.Biochemical Society transactions · 2016Review
- Efficient Chemoenzymatic Synthesis of an N-glycan Isomer Library.Chemical science · 2015Article
- Efficient chemoenzymatic synthesis of novel galacto-N-biose derivatives and their sialylated forms.Chemical communications (Cambridge, England) · 2015Article
- Human Milk Oligosaccharides (HMOS): Structure, Function, and Enzyme-Catalyzed Synthesis.Advances in carbohydrate chemistry and biochemistry · 2015Review
- Crystal structures of sialyltransferase from Photobacterium damselae.FEBS letters · 2014Article
- Review
- One-pot multi-enzyme (OPME) chemoenzymatic synthesis of sialyl-Tn-MUC1 and sialyl-T-MUC1 glycopeptides containing natural or non-natural sialic acid.Bioorganic & medicinal chemistry · 2013Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Pasteurella multocida α2-3-sialyltransferase 1 (PmST1) is a multifunctional enzyme which has α2-6-sialyltransferase, α2-3-sialidase, and α2-3-trans-sialidase activities in addition to its major α2-3-sialyltransferase activity. The presence of the α2-3-sialidase activity of PmST1 complicates its application in enzymatic synthesis of α2-3-linked sialosides as the product formed can be hydrolyzed by the enzyme. Herein we show that the α2-3-sialidase activity of PmST1 can be significantly decreased by protein crystal structure-based site-directed mutagenesis. A PmST1 double mutant E271F/R313Y showed a significantly (6333-fold) decreased sialidase activity without affecting its α2-3-sialyltransferase activity. The double mutant E271F/R313Y, therefore, is a superior enzyme for enzymatic synthesis of α2-3-linked sialosides.
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Registered trials
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