ArticleNature communications2021
Physical constraints and functional plasticity of cellulases.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Effect of composite-enzymatically modified Ganoderma lucidum powder on rheological and structural properties of soft wheat flour dough and cookie quality.Journal of the science of food and agriculture · 2026Article
- Stoichiometrically Engineered Hydrated Ionic Liquids Enabling Reinforcement of Enzyme Cascade with Improved Thermodynamic Stability.ACS sustainable chemistry & engineering · 2026Article
- Reduced Processivity in a Chitobiohydrolase Enhances LPMO-Assisted Chitin Depolymerization.Biochemistry · 2026Article
- Kinetic Dissection of the Reaction of Human GDP-l-Fucose Synthase.ACS catalysis · 2025Article
- The Sabatier principle governs the performance of self-sufficient heterogeneous biocatalysts for redox biotransformations.Cell reports. Physical science · 2025Article
- Molecular Details of Polyester Decrystallization via Molecular Simulation.Macromolecules · 2025Article
- Article
- Engineering of glycoside hydrolase family 7 cellobiohydrolases directed by natural diversity screening.The Journal of biological chemistry · 2024Article
- Improving stereoselectivity of phosphotriesterase (PTE) for kinetic resolution of chiral phosphates.Frontiers in bioengineering and biotechnology · 2024Article
- Thermodynamic principle to enhance enzymatic activity using the substrate affinity.Nature communications · 2023Article
- Engineering cellulases for conversion of lignocellulosic biomass.Protein engineering, design & selection : PEDS · 2023Review
- Acoustic force spectroscopy reveals subtle differences in cellulose unbinding behavior of carbohydrate-binding modules.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Fungal cellulases: protein engineering and post-translational modifications.Applied microbiology and biotechnology · 2022Review
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Authors and funding
19 authors.
Funding
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Abstract
Enzyme reactions, both in Nature and technical applications, commonly occur at the interface of immiscible phases. Nevertheless, stringent descriptions of interfacial enzyme catalysis remain sparse, and this is partly due to a shortage of coherent experimental data to guide and assess such work. In this work, we produced and kinetically characterized 83 cellulases, which revealed a conspicuous linear free energy relationship (LFER) between the substrate binding strength and the activation barrier. The scaling occurred despite the investigated enzymes being structurally and mechanistically diverse. We suggest that the scaling reflects basic physical restrictions of the hydrolytic process and that evolutionary selection has condensed cellulase phenotypes near the line. One consequence of the LFER is that the activity of a cellulase can be estimated from its substrate binding strength, irrespectively of structural and mechanistic details, and this appears promising for in silico selection and design within this industrially important group of enzymes.
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