Systematic investigation of the link between enzyme catalysis and cold adaptation
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...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
eLife Sciences Publications Ltd
2022-01-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/72884 |
| _version_ | 1811199872867500032 |
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| author | Catherine Stark Teanna Bautista-Leung Joanna Siegfried Daniel Herschlag |
| author_facet | Catherine Stark Teanna Bautista-Leung Joanna Siegfried Daniel Herschlag |
| author_sort | Catherine Stark |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T01:54:48Z |
| format | Article |
| id | doaj.art-7232d1e166e04c89a5f1be99f31e7c3f |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T01:54:48Z |
| publishDate | 2022-01-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-7232d1e166e04c89a5f1be99f31e7c3f2022-12-22T03:52:49ZengeLife Sciences Publications LtdeLife2050-084X2022-01-011110.7554/eLife.72884Systematic investigation of the link between enzyme catalysis and cold adaptationCatherine Stark0https://orcid.org/0000-0002-0848-3858Teanna Bautista-Leung1Joanna Siegfried2Daniel Herschlag3https://orcid.org/0000-0002-4685-1973ChEM-H, Stanford University, Stanford, United States; Department of Biochemistry, Stanford University, Stanford, United StatesDepartment of Biochemistry, Stanford University, Stanford, United StatesDepartment of Biochemistry, Stanford University, Stanford, United StatesChEM-H, Stanford University, Stanford, United States; Department of Biochemistry, Stanford University, Stanford, United States; Department of Chemical Engineering, Stanford University, Stanford, United StatesCold 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.https://elifesciences.org/articles/72884enzyme ratecold adaptationevolutionary biochemistry |
| spellingShingle | Catherine Stark Teanna Bautista-Leung Joanna Siegfried Daniel Herschlag Systematic investigation of the link between enzyme catalysis and cold adaptation eLife enzyme rate cold adaptation evolutionary biochemistry |
| title | Systematic investigation of the link between enzyme catalysis and cold adaptation |
| title_full | Systematic investigation of the link between enzyme catalysis and cold adaptation |
| title_fullStr | Systematic investigation of the link between enzyme catalysis and cold adaptation |
| title_full_unstemmed | Systematic investigation of the link between enzyme catalysis and cold adaptation |
| title_short | Systematic investigation of the link between enzyme catalysis and cold adaptation |
| title_sort | systematic investigation of the link between enzyme catalysis and cold adaptation |
| topic | enzyme rate cold adaptation evolutionary biochemistry |
| url | https://elifesciences.org/articles/72884 |
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