ArticleACS chemical biology2018
α2-6-Neosialidase: A Sialyltransferase Mutant as a Sialyl Linkage-Specific Sialidase.
Article in ACS chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Mammalian Cell Surface Display for High-Throughput Protein Engineering of Glycosyltransferases.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Enzyme cascades for nucleotide sugar regeneration in glycoconjugate synthesis.Applied microbiology and biotechnology · 2025Review
- Synthetic Catalysts for Selective Glycan Cleavage from Glycoproteins and Cells.Journal of the American Chemical Society · 2024Article
- Enabling Chemoenzymatic Strategies and Enzymes for Synthesizing Sialyl Glycans and Sialyl Glycoconjugates.Accounts of chemical research · 2024Article
- Sialosides Containing 7-ACS infectious diseases · 2023Article
- Cellular and Molecular Engineering of Glycan Sialylation in Heterologous Systems.Molecules (Basel, Switzerland) · 2021Review
- An α2,3-Sialyltransferase from Photobacterium phosphoreum with Broad Substrate Scope: Controlling Hydrolytic Activity by Directed Evolution.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- EngineerACS catalysis · 2020Article
- 9-Azido-9-deoxy-2,3-difluorosialic Acid as a Subnanomolar Inhibitor against Bacterial Sialidases.The Journal of organic chemistry · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The lack of α2-6-linkage specific sialidases limits the structural and functional studies of sialic-acid-containing molecules. Photobacterium damselae α2-6-sialyltransferase (Pd2,6ST) was shown previously to have α2-6-specific, but weak, sialidase activity. Here, we develop a high-throughput blue-white colony screening method to identify Pd2,6ST mutants with improved α2-6-sialidase activity from mutant libraries generated by sequential saturation mutagenesis. A triple mutant (Pd2,6ST S232L/T356S/W361F) has been identified with 100-fold improved activity, high α2-6-sialyl linkage selectivity, and ability to cleave two common sialic acid forms, N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc). It is a valuable tool for sialoglycan structural analysis and functional characterization. The sequential saturation mutagenesis and screening strategy developed here can be explored to evolve other linkage-specific neoglycosidases from the corresponding glycosyltransferases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.