ArticleBiochemistry2022
The Activation Parameters of a Cold-Adapted Short Chain Dehydrogenase Are Insensitive to Enzyme Oligomerization.
Article in Biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 13 citations in OpenAlex.
- Genomic signatures of cold adaptation in a Himalayan drosophilid.G3 (Bethesda, Md.) · 2026Article
- Enhancing Cold Adaptation of Bidomain Amylases by High-Throughput Computational Engineering.Angewandte Chemie (International ed. in English) · 2025Article
- Quaternary stabilization of a GH2 β-galactosidase from the psychrophile A. ikkensis, a flexible and unstable dimeric enzyme.Protein science : a publication of the Protein Society · 2025Article
- Computer Simulations of the Temperature Dependence of Enzyme Reactions.Journal of chemical theory and computation · 2025Review
- Computational Analysis of Heat Capacity Effects in Protein-Ligand Binding.Journal of chemical theory and computation · 2024Article
- Why Do Empirical Valence Bond Simulations Yield Accurate Arrhenius Plots?Journal of chemical theory and computation · 2024Article
- Helping proteins come in from the cold: 5 burning questions about cold-active enzymes.BBA advances · 2024Review
- Efficient Empirical Valence Bond Simulations with GROMACS.Journal of chemical theory and computation · 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
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The structural principles of enzyme cold adaptation are of fundamental interest both for understanding protein evolution and for biotechnological applications. It has become clear in recent years that structural flexibility plays a major role in tuning enzyme activity at low temperatures, which is reflected by characteristic changes in the thermodynamic activation parameters for psychrophilic enzymes, compared to those of mesophilic and thermophilic ones. Hence, increased flexibility of the enzyme surface has been shown to lead to a lower enthalpy and a more negative entropy of activation, which leads to higher activity in the cold. This immediately raises the question of how enzyme oligomerization affects the temperature dependence of catalysis. Here, we address this issue by computer simulations of the catalytic reaction of a cold-adapted bacterial short chain dehydrogenase in different oligomeric states. Reaction free energy profiles are calculated at different temperatures for the tetrameric, dimeric, and monomeric states of the enzyme, and activation parameters are obtained from the corresponding computational Arrhenius plots. The results show that the activation free energy, enthalpy, and entropy are remarkably insensitive to the oligomeric state, leading to the conclusion that assembly of the subunit interfaces does not compromise cold adaptation, even though the mobilities of interfacial residues are indeed affected.
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