ArticleNature communications2019
Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Report of the 5th International Symposium on Frontiers in Molecular Science (ISFMS 2025).International journal of molecular sciences · 2025Article
- The structure and dynamics of water molecule networks underlie catalytic efficiency in a glycoside exo-hydrolase.Communications biology · 2025Article
- A functionally augmented carbohydrate utilization locus from herbivore gut microbiota fueled by dietary β-glucans.NPJ biofilms and microbiomes · 2024Article
- Enzymes in 3D: Synthesis, remodelling, and hydrolysis of cell wall (1,3;1,4)-β-glucans.Plant physiology · 2023Article
- The Discovery of the Fucoidan-Active Endo-1→4-α-L-Fucanase of the GH168 Family, Which Produces Fucoidan Derivatives with Regular Sulfation and Anticoagulant Activity.International journal of molecular sciences · 2023Article
- Geometric Remodeling of Nitrilase Active Pocket Based on ALF-Scanning Strategy To Enhance Aromatic Nitrile Substrate Preference and Catalytic Efficiency.Applied and environmental microbiology · 2023Article
- Molecular mechanisms of processive glycoside hydrolases underline catalytic pragmatism.Biochemical Society transactions · 2023Article
- Drug Design in the Exascale Era: A Perspective from Massively Parallel QM/MM Simulations.Journal of chemical information and modeling · 2023Review
- Tuning Selectivity in CalA Lipase: Beyond Tunnel Engineering.Biochemistry · 2023Article
- The evolutionary advantage of an aromatic clamp in plant family 3 glycoside exo-hydrolases.Nature communications · 2022Article
- Research progress and the biotechnological applications of multienzyme complex.Applied microbiology and biotechnology · 2021Review
- GPathFinder: Identification of Ligand-Binding Pathways by a Multi-Objective Genetic Algorithm.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
20 authors at 10 institutions in 7 countries.
Funding
Abstract
Substrates associate and products dissociate from enzyme catalytic sites rapidly, which hampers investigations of their trajectories. The high-resolution structure of the native Hordeum exo-hydrolase HvExoI isolated from seedlings reveals that non-covalently trapped glucose forms a stable enzyme-product complex. Here, we report that the alkyl β-D-glucoside and methyl 6-thio-β-gentiobioside substrate analogues perfused in crystalline HvExoI bind across the catalytic site after they displace glucose, while methyl 2-thio-β-sophoroside attaches nearby. Structural analyses and multi-scale molecular modelling of nanoscale reactant movements in HvExoI reveal that upon productive binding of incoming substrates, the glucose product modifies its binding patterns and evokes the formation of a transient lateral cavity, which serves as a conduit for glucose departure to allow for the next catalytic round. This path enables substrate-product assisted processive catalysis through multiple hydrolytic events without HvExoI losing contact with oligo- or polymeric substrates. We anticipate that such enzyme plasticity could be prevalent among exo-hydrolases.
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Registered trials
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