ArticleInternational journal of molecular sciences2023
Molecular Dynamics Simulations Reveal the Conformational Transition of GH33 Sialidases.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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
5 citing papers in PubMed, 6 citations in OpenAlex.
- From cognition to response: clinical challenges, antibiotic resistance mechanisms, and prevention and control strategies ofFrontiers in microbiology · 2026Review
- Semi-rational engineering of an α-L-fucosidase for regioselective synthesis of fucosyl-Food chemistry. Molecular sciences · 2025Article
- Structural and functional insights into metal coordination and substrate recognition of Akkermansia muciniphila sialidase Amuc_1547.Molecular biomedicine · 2025Article
- Mining versatile feruloyl esterases: phylogenetic classification, structural features, and deep learning model.Bioresources and bioprocessing · 2025Article
- Computational toolbox for the analysis of protein-glycan interactions.Beilstein journal of organic chemistry · 2024Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Sialidases are increasingly used in the production of sialyloligosaccharides, a significant component of human milk oligosaccharides. Elucidating the catalytic mechanism of sialidases is critical for the rational design of better biocatalysts, thereby facilitating the industrial production of sialyloligosaccharides. Through comparative all-atom molecular dynamics simulations, we investigated the structural dynamics of sialidases in Glycoside Hydrolase family 33 (GH33). Interestingly, several sialidases displayed significant conformational transition and formed a new cleft in the simulations. The new cleft was adjacent to the innate active site of the enzyme, which serves to accommodate the glycosyl acceptor. Furthermore, the residues involved in the specific interactions with the substrate were evolutionarily conserved in the whole GH33 family, highlighting their key roles in the catalysis of GH33 sialidases. Our results enriched the catalytic mechanism of GH33 sialidases, with potential implications in the rational design of sialidases.
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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 Socratic graph.