ArticleScientific reports2019
Towards Rational Computational Engineering of Psychrophilic Enzymes.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Discovery of a cryptic aminoacidic triad involved in the temperature adaptation of GH1 enzymes.The FEBS journal · 2026Article
- Enhancing Cold Adaptation of Bidomain Amylases by High-Throughput Computational Engineering.Angewandte Chemie (International ed. in English) · 2025Article
- Cold-Active Starch-Degrading Enzymes from a Cold and Alkaline Greenland Environment: Role of CaBiomolecules · 2025Article
- Computer Simulations of the Temperature Dependence of Enzyme Reactions.Journal of chemical theory and computation · 2025Review
- Metagenomic exploration of cold-active enzymes for detergent applications: Characterization of a novel, cold-active and alkali-stable GH8 endoglucanase from ikaite columns in SW Greenland.Microbial biotechnology · 2024Article
- Helping proteins come in from the cold: 5 burning questions about cold-active enzymes.BBA advances · 2024Review
- A general overview of the multifactorial adaptation to cold: biochemical mechanisms and strategies.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Review
- Glycosylation increases active site rigidity leading to improved enzyme stability and turnover.The FEBS journal · 2023Article
- Computational design of the temperature optimum of an enzyme reaction.Science advances · 2023Article
- Principles of Cold Adaptation of Fish Lactate Dehydrogenases Revealed by Computer Simulations of the Catalytic Reaction.Molecular biology and evolution · 2023Article
- Role of Enzyme and Active Site Conformational Dynamics in the Catalysis by α-Amylase Explored with QM/MM Molecular Dynamics.Journal of chemical information and modeling · 2022Article
- Structure and Mechanism of a Cold-Adapted Bacterial Lipase.Biochemistry · 2022Article
- The Activation Parameters of a Cold-Adapted Short Chain Dehydrogenase Are Insensitive to Enzyme Oligomerization.Biochemistry · 2022Article
- Chemical Mapping Exposes the Importance of Active Site Interactions in Governing the Temperature Dependence of Enzyme Turnover.ACS catalysis · 2021Article
- Psychrophilic enzymes: structural adaptation, pharmaceutical and industrial applications.Applied microbiology and biotechnology · 2021Review
- The Energetic Origin of Different Catalytic Activities in Temperature-Adapted Trypsins.ACS omega · 2020Article
- Computer simulations explain the anomalous temperature optimum in a cold-adapted enzyme.Nature communications · 2020Article
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4 authors.
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Abstract
Cold-adapted enzymes from psychrophilic species achieve their high catalytic efficiency at low temperature by a different partitioning of the activation free energy into its enthalpic and entropic components, compared to orthologous mesophilic enzymes. Their lower activation enthalpy, partly compensated by an increased entropic penalty, has been suggested to originate from changes in flexibility of the protein surface. Multiple sequence alignments of psychrophilic and mesophilic enzymes also show characteristic motifs located in surface loops of the protein. Here, we use computer simulations to examine the effects of a number of designed surface mutations of psychrophilic and mesophilic elastases on the temperature dependence of the catalyzed peptide cleavage reaction. For each of 14 mutant enzyme variants we report calculations of their thermodynamic activation parameters. The results show that substitution of psychrophilic loop residues into the mesophilic enzyme consistently changes both the activation parameters and loop flexibilities towards the former, and vice versa for opposite substitutions.
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