ArticleScientific reports2019
Establishment of mesophilic-like catalytic properties in a thermophilic enzyme without affecting its thermal stability.
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 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- How far can you go? Extrapolating values of catalytic activity from known protein landscapes in natural and directed evolution.Chemical Society reviews · 2026Review
- One-site polarity switch enhances catalytic efficiency and stability of D-allulose 3-epimerase via flexibility-rigidity rebalancing.Scientific reports · 2026Article
- Targeted mutagenesis of a thermophilic mevalonate kinase for efficient catalysis at lower temperatures.Protein engineering, design & selection : PEDS · 2026Article
- Article
- Catalytic His-loop flexibility drives high activity in hyperthermophilic esterase EstE1 while preserving structural stability.Microbiology spectrum · 2025Article
- Insights into the low-temperature adaptation of an enzyme as studied through ancestral sequence reconstruction.Protein science : a publication of the Protein Society · 2025Article
- Low-temperature features of the psychrophilic chaperonin from Pseudoalteromonas haloplanktis.Archives of microbiology · 2024Article
- Engineering and application of LacI mutants with stringent expressions.Microbial biotechnology · 2024Article
- Understanding activity-stability tradeoffs in biocatalysts by enzyme proximity sequencing.Nature communications · 2024Article
- Lignocellulolytic extremozymes and their biotechnological applications.Extremophiles : life under extreme conditions · 2023Review
- Enzyme dynamics-a brief review.Biophysical reviews · 2023Article
- Improving Both the Thermostability and Catalytic Efficiency of Phospholipase D fromInternational journal of molecular sciences · 2022Article
- Double mutations far from the active site affect cold activity in an Antarctic halophilic β-galactosidase.Protein science : a publication of the Protein Society · 2022Article
- Chemical Mapping Exposes the Importance of Active Site Interactions in Governing the Temperature Dependence of Enzyme Turnover.ACS catalysis · 2021Article
- Structure, Function, and Thermodynamics of Lactate Dehydrogenases from Humans and the Malaria ParasiteBiochemistry · 2021Article
- Kinetic Analysis Suggests Evolution of Ribosome Specificity in Modern Elongation Factor-Tus from "Generalist" Ancestors.Molecular biology and evolution · 2021Article
- The high-energy transition state of the glutamate transporter homologue GltPh.The EMBO journal · 2021Article
- Novel Thermophilic Bacterial Laccase for the Degradation of Aromatic Organic Pollutants.Frontiers in chemistry · 2021Article
- Ancestral sequence reconstruction produces thermally stable enzymes with mesophilic enzyme-like catalytic properties.Scientific reports · 2020Article
- Manganese(II) Oxidizing Bacteria as Whole-Cell Catalyst for β-Keto Ester Oxidation.International journal of molecular sciences · 2020Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermophilic enzymes are generally more thermally stable but are less active at moderate temperatures than are their mesophilic counterparts. Thermophilic enzymes with improved low-temperature activity that retain their high stability would serve as useful tools for industrial processes especially when robust biocatalysts are required. Here we show an effective way to explore amino acid substitutions that enhance the low-temperature catalytic activity of a thermophilic enzyme, based on a pairwise sequence comparison of thermophilic/mesophilic enzymes. One or a combination of amino acid(s) in 3-isopropylmalate dehydrogenase from the extreme thermophile Thermus thermophilus was/were substituted by a residue(s) found in the Escherichia coli enzyme at the same position(s). The best mutant, which contained three amino acid substitutions, showed a 17-fold higher specific activity at 25 °C compared to the original wild-type enzyme while retaining high thermal stability. The kinetic and thermodynamic parameters of the mutant showed similar patterns along the reaction coordinate to those of the mesophilic enzyme. We also analyzed the residues at the substitution sites from a structural and phylogenetic point of view.
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