ReviewJournal of chemical theory and computation2025
Computer Simulations of the Temperature Dependence of Enzyme Reactions.
Review in Journal of chemical theory and computation, 2025. 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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Who cites it
5 citing papers in PubMed.
- Discovery of a cryptic aminoacidic triad involved in the temperature adaptation of GH1 enzymes.The FEBS journal · 2026Article
- Activation parameters, enthalpy-entropy compensation and the temperature-dependent activity of enzymes.Protein science : a publication of the Protein Society · 2026Article
- Thermodynamic Activation Parameters for Chemical Reactions in Enzymes and Solution from Computer Simulations at a Single Temperature.Journal of chemical theory and computation · 2026Article
- Activation parameters, enthalpy-entropy compensation and the temperature-dependent activity of enzymes.bioRxiv : the preprint server for biology · 2025Article
- Approaches for regulating enzyme activities: Recent advances in experiment and computation.Current opinion in structural biology · 2025Review
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Authors and funding
2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
In this review we discuss the development of methodology for calculating the temperature dependence and thermodynamic activation parameters for chemical reactions in solution and in enzymes, from computer simulations. We outline how this is done by combining the empirical valence bond method with molecular dynamics free energy simulations. In favorable cases it turns out that such simulations can even capture temperature optima for the catalytic rate. The approach turns out be very useful both for addressing questions regarding the roles of enthalpic and entropic effects in specific enzymes and also for attacking evolutionary problems regarding enzyme adaptation to different temperature regimes. In the latter case, we focus on cold-adaptation of enzymes from psychrophilic species and show how computer simulations have revealed the basic mechanisms behind such adaptation. Understanding these mechanisms also opens up the possibility of designing the temperature dependence, and we highlight a recent example of this.
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