ArticleNature communications2025
Unraveling the molecular mechanism of polysaccharide lyases for efficient alginate degradation.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Unraveling A4GALT Mechanism and Its Modulation With Adamantyl-Galactosylceramide Analogues: Advancing Fabry Disease Therapeutic Strategies.Angewandte Chemie (International ed. in English) · 2026Article
- Functionalized bio-patches for intra-abdominal applications.iScience · 2026Review
- Efficient QM/MM Modeling of Enzymatic Reactions Combining PathCV with OPES.Journal of chemical theory and computation · 2026Article
- Untangling the Reaction Mechanism of the Polysaccharide Lyase PL42 Using QM/MM Metadynamics Simulations.Journal of chemical information and modeling · 2026Article
- Catalyzing Carbohydrate Cleavage: Glycosidases and Their Mechanisms.Chemical reviews · 2026Review
- Unravelling Rheology and Structural Properties of Polysaccharides from Porphyridium Purpureum After Alkali Pre-Treatment.Macromolecular bioscience · 2026Article
- Alginate-Based Hydrogels: Recent Progress in Preparation, Property Tuning, and Multifunctional Applications.Gels (Basel, Switzerland) · 2026Review
- Enhanced Thermostability and Catalytic Efficiency of Alginate Lyase Alyw203 by Hydrogen Bond Network Reconstruction.Marine drugs · 2025Article
- Methionine Salvage Enzyme Uses a Unique Mechanism to Overcome a Challenging Aldose-Ketose Isomerization.Journal of the American Chemical Society · 2025Article
- Alginate oligosaccharides in the food industry: emerging functional roles, health benefits, and technological applications - Review.Food chemistry: X · 2025Review
- Exploring the Catalytic Mechanisms of a Newly Identified Salt-Activated Alginate Lyase fromMarine drugs · 2025Article
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Authors and funding
13 authors.
Funding
Abstract
Alginate lyases (ALs) catalyze the depolymerization of brown macroalgae alginates, widely used naturally occurring polysaccharides. Their molecular reaction mechanism remains elusive due to the lack of catalytically competent Michaelis-Menten-like complex structures. Here, we provide structural snapshots and dissect the mechanism of mannuronan-specific ALs from family 7 polysaccharide lyases (PL7), employing time-resolved NMR, X-ray, neutron crystallography, and QM/MM simulations. We reveal the protonation state of critical active site residues, enabling atomic-level analysis of the reaction coordinate. Our approach reveals an endolytic and asynchronous syn β-elimination reaction, with Tyr serving as both Brønsted base and acid, involving a carbanion-type transition state. This study not only reconciles previous structural and kinetic discrepancies, but also establishes a comprehensive PL reaction mechanism which is most likely applicable across all enzymes of the PL7 family as well as other PL families.
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