ArticleNature communications2018
Dynamical origins of heat capacity changes in enzyme-catalysed reactions.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.
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Who cites it
45 citing papers in PubMed, 1 synthesis or guideline pooled it, 91 citations in OpenAlex.
- A meta-analysis of the activity, stability, and mutational characteristics of temperature-adapted enzymes.Bioscience reports · 2021Pooled it
- Domain shuffling of endolysin LysKB317 to controlBiotechnology reports (Amsterdam, Netherlands) · 2026Article
- Discovery of a cryptic aminoacidic triad involved in the temperature adaptation of GH1 enzymes.The FEBS journal · 2026Article
- Analysis of the Atypical Temperature Dependence and Conformational Changes During Turnover of a Lactobacillus Chlorogenic Acid Esterase.Biochemistry · 2026Article
- Activation parameters, enthalpy-entropy compensation and the temperature-dependent activity of enzymes.Protein science : a publication of the Protein Society · 2026Article
- Catalytic Promiscuity and Cascade Reaction Mechanism of Ketosteroid Isomerases for Addition Reactions of Cyclic Enones.Nature communications · 2026Article
- Mechanistic basis for improved activity of Engineered AsCas12a.Communications biology · 2026Article
- Identification of novel triazolopyrimidines as potent α-glucosidase inhibitor through design, synthesis, biological evaluations, and computational analysis.Scientific reports · 2025Article
- Buttressing ligand-binding pockets in de novo designed NTF2-like domains.Protein science : a publication of the Protein Society · 2025Article
- SubTuner leverages physics-based modeling to complement AI in enzyme engineering toward non-native substrates.Chem catalysis · 2025Article
- Design, synthesis, and investigation of novel 5-arylpyrazole-glucose hybrids as α-glucosidase inhibitors.Scientific reports · 2025Article
- Biofunctionalization of Magneto-Plasmonic FeMolecules (Basel, Switzerland) · 2025Article
- Broad substrate scope C-C oxidation in cyclodipeptides catalysed by a flavin-dependent filament.Nature communications · 2025Article
- A minimal biophysical model for the temperature dependence of CO2 fixation rates based on macromolecular rate theory.PloS one · 2025Article
- A structural perspective on the temperature-dependent activity of enzymes.bioRxiv : the preprint server for biology · 2024Article
- Computational Analysis of Heat Capacity Effects in Protein-Ligand Binding.Journal of chemical theory and computation · 2024Article
- Interplay of structural preorganization and conformational sampling in UDP-glucuronic acid 4-epimerase catalysis.Nature communications · 2024Article
- Cooperative Conformational Transitions Underpin the Activation Heat Capacity in the Temperature Dependence of Enzyme Catalysis.ACS catalysis · 2024Article
- Snapshots of the Reaction Coordinate of a Thermophilic 2'-Deoxyribonucleoside/ribonucleoside Transferase.ACS catalysis · 2024Article
- Polymorphic positions 349 and 725 of the autoimmunity-protective allotype 10 of ER aminopeptidase 1 are key in determining its unique enzymatic properties.Frontiers in immunology · 2024Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Heat capacity changes are emerging as essential for explaining the temperature dependence of enzyme-catalysed reaction rates. This has important implications for enzyme kinetics, thermoadaptation and evolution, but the physical basis of these heat capacity changes is unknown. Here we show by a combination of experiment and simulation, for two quite distinct enzymes (dimeric ketosteroid isomerase and monomeric alpha-glucosidase), that the activation heat capacity change for the catalysed reaction can be predicted through atomistic molecular dynamics simulations. The simulations reveal subtle and surprising underlying dynamical changes: tightening of loops around the active site is observed, along with changes in energetic fluctuations across the whole enzyme including important contributions from oligomeric neighbours and domains distal to the active site. This has general implications for understanding enzyme catalysis and demonstrating a direct connection between functionally important microscopic dynamics and macroscopically measurable quantities.
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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.