ArticleBiochemistry2007
On the relationship between thermal stability and catalytic power of enzymes.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Trylons: Polyamide Surrogate Substrates Enable High-Throughput Screening of Nylon-Degrading Enzymes.Chembiochem : a European journal of chemical biology · 2026Article
- One-site polarity switch enhances catalytic efficiency and stability of D-allulose 3-epimerase via flexibility-rigidity rebalancing.Scientific reports · 2026Article
- Enhancing Bacillus cereus antibacterial ability through improved cofactor supply.Microbial cell factories · 2025Article
- Structure and stability of an apo thermophilic esterase that hydrolyzes polyhydroxybutyrate.Acta crystallographica. Section D, Structural biology · 2024Article
- Harnessing generative AI to decode enzyme catalysis and evolution for enhanced engineering.National science review · 2023Review
- Harnessing Generative AI to Decode Enzyme Catalysis and Evolution for Enhanced Engineering.bioRxiv : the preprint server for biology · 2023Article
- A porphyrin-based molecular cage guided by designed local-electric field is highly selective and efficient.Chemical science · 2023Article
- Enzyme dynamics-a brief review.Biophysical reviews · 2023Article
- Bioplastic degradation by a polyhydroxybutyrate depolymerase from a thermophilic soil bacterium.Protein science : a publication of the Protein Society · 2022Article
- Natural Evolution Provides Strong Hints about Laboratory Evolution of Designer Enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Enhancing computational enzyme design by a maximum entropy strategy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Simple Method of Preparation of Highly Carboxylated Bacterial Cellulose with Ni- and Mg-Ferrite-Based Versatile Magnetic Carrier for Enzyme Immobilization.International journal of molecular sciences · 2021Article
- Electrostatic interaction optimization improves catalytic rates and thermotolerance on xylanases.Biophysical journal · 2021Article
- Directional conformer exchange in dihydrofolate reductase revealed by single-molecule nanopore recordings.Nature chemistry · 2020Article
- The Role of Electrostatics and Folding Kinetics on the Thermostability of Homologous Cold Shock Proteins.Journal of chemical information and modeling · 2020Article
- Distinct roles of an ionic interaction holding an alpha-helix with catalytic Asp and a beta-strand with catalytic His in a hyperthermophilic esterase EstE1 and a mesophilic esterase rPPE.Extremophiles : life under extreme conditions · 2019Article
- Why are some Enzymes Dimers? Flexibility and Catalysis inACS catalysis · 2019Article
- Effects of pH and Salt Concentration on Stability of a Protein G Variant Using Coarse-Grained Models.Biophysical journal · 2018Article
- Sortase A-mediated crosslinked short-chain dehydrogenases/reductases as novel biocatalysts with improved thermostability and catalytic efficiency.Scientific reports · 2017Article
- Perspective: Defining and quantifying the role of dynamics in enzyme catalysis.The Journal of chemical physics · 2016Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The possible relationship between the thermal stability and the catalytic power of enzymes is of great current interest. In particular, it has been suggested that thermophilic or hyperthermophilic (Tm) enzymes have lower catalytic power at a given temperature than the corresponding mesophilic (Ms) enzymes, because the thermophilic enzymes are less flexible (assuming that flexibility and catalysis are directly correlated). These suggestions presume that the reduced dynamics of the thermophilic enzymes is the reason for their reduced catalytic power. The present paper takes the specific case of dihydrofolate reductase (DHFR) and explores the validity of the above argument by simulation approaches. It is found that the Tm enzymes have restricted motions in the direction of the folding coordinate, but this is not relevant to the chemical process, since the motions along the reaction coordinate are perpendicular to the folding motions. Moreover, it is shown that the rate of the chemical reaction is determined by the activation barrier and the corresponding reorganization energy, rather than by dynamics or flexibility in the ground state. In fact, as far as flexibility is concerned, we conclude that the displacement along the reaction coordinate is larger in the Tm enzyme than in the Ms enzyme and that the general trend in enzyme catalysis is that the best catalyst involves less motion during the reaction than the less optimal catalyst. The relationship between thermal stability and catalysis appears to reflect the fact that to obtain small electrostatic reorganization energy it is necessary to invest some folding energy in the overall preorganization process. Thus, the optimized catalysts are less stable. This trend is clearly observed in the DHFR case.
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Registered trials
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