Systematic investigation of the link between enzyme catalysis and cold adaptation
| العنوان: | Systematic investigation of the link between enzyme catalysis and cold adaptation |
|---|---|
| المؤلفون: | Joanna Siegfried, Teanna Bautista-Leung, Catherine D. Stark, Daniel Herschlag |
| المصدر: | eLife, Vol 11 (2022) eLife |
| بيانات النشر: | eLife Sciences Publications Ltd, 2022. |
| سنة النشر: | 2022 |
| مصطلحات موضوعية: | QH301-705.5, Science, Short Report, Isomerase, evolutionary biochemistry, General Biochemistry, Genetics and Molecular Biology, Catalysis, Enzyme catalysis, chemistry.chemical_compound, Biochemistry and Chemical Biology, Ketosteroid, None, Biology (General), chemistry.chemical_classification, biology, General Immunology and Microbiology, Chemistry, General Neuroscience, Active site, General Medicine, Adaptation, Physiological, Enzymes, Cold Temperature, Enzyme, enzyme rate, cold adaptation, biology.protein, Biophysics, Medicine, Adaptation, Function (biology) |
| الوصف: | Cold temperature is prevalent across the biosphere and slows the rates of chemical reactions. Increased catalysis has been predicted to be a dominant adaptive trait of enzymes to reduced temperature, and this expectation has informed physical models for enzyme catalysis and influenced bioprospecting strategies. To systematically test rate enhancement as an adaptive trait to cold, we paired kinetic constants of 2223 enzyme reactions with their organism’s optimal growth temperature (TGrowth) and analyzed trends of rate constants as a function of TGrowth. These data do not support a general increase in rate enhancement in cold adaptation. In the model enzyme ketosteroid isomerase (KSI), there is prior evidence for temperature adaptation from a change in an active site residue that results in a tradeoff between activity and stability. Nevertheless, we found that little of the rate constant variation for 20 KSI variants was accounted for by TGrowth. In contrast, and consistent with prior expectations, we observed a correlation between stability and TGrowth across 433 proteins. These results suggest that temperature exerts a weaker selection pressure on enzyme rate constants than stability and that evolutionary forces other than temperature are responsible for the majority of enzymatic rate constant variation. |
| اللغة: | English |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb60f78a24cf877aba4b827267dbdea4Test https://elifesciences.org/articles/72884Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....cb60f78a24cf877aba4b827267dbdea4 |
| قاعدة البيانات: | OpenAIRE |
| الوصف غير متاح. |