ArticleBiochemistry2014
Thermal adaptation of dihydrofolate reductase from the moderate thermophile Geobacillus stearothermophilus.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- Unlocking the molecular engineering of Geobacillus glycoside hydrolases as a source of industrial biocatalysts.Biotechnology letters · 2026Review
- Cryo-kinetics Reveal Dynamic Effects on the Chemistry of Human Dihydrofolate Reductase.Chembiochem : a European journal of chemical biology · 2021Article
- Parallel molecular mechanisms for enzyme temperature adaptation.Science (New York, N.Y.) · 2021Article
- A Method for Prediction of Thermophilic Protein Based on Reduced Amino Acids and Mixed Features.Frontiers in bioengineering and biotechnology · 2020Article
- Halophilic mechanism of the enzymatic function of a moderately halophilic dihydrofolate reductase from Haloarcula japonica strain TR-1.Extremophiles : life under extreme conditions · 2017Article
- Minimization of dynamic effects in the evolution of dihydrofolate reductase.Chemical science · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The thermal melting temperature of dihydrofolate reductase from Geobacillus stearothermophilus (BsDHFR) is ~30 °C higher than that of its homologue from the psychrophile Moritella profunda. Additional proline residues in the loop regions of BsDHFR have been proposed to enhance the thermostability of BsDHFR, but site-directed mutagenesis studies reveal that these proline residues contribute only minimally. Instead, the high thermal stability of BsDHFR is partly due to removal of water-accessible thermolabile residues such as glutamine and methionine, which are prone to hydrolysis or oxidation at high temperatures. The extra thermostability of BsDHFR can be obtained by ligand binding, or in the presence of salts or cosolvents such as glycerol and sucrose. The sum of all these incremental factors allows BsDHFR to function efficiently in the natural habitat of G. stearothermophilus, which is characterized by temperatures that can reach 75 °C.
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Registered trials
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