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A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
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Evolutionary drivers of thermoadaptation in enzyme catalysis
Vy Nguyen1, Christopher Wilson1, Marc Hoemberger1
1Howard Hughes Medical Institute and Department of Biochemistry, Brandeis University, Waltham, MA 02452, USA.
Science (New York, N.Y.)
|December 24, 2016
Summary
Enzymes evolved to maintain catalytic speed in cooler temperatures by utilizing transition-state heat capacity. This study reveals molecular mechanisms of thermoadaptation in adenylate kinase across 3 billion years of evolution.
Area of Science:
- Biochemistry
- Evolutionary Biology
- Molecular Biology
Background:
- Early life evolved in hot environments, posing challenges for enzyme function as temperatures decreased.
- Enzymes need to maintain catalytic efficiency despite temperature fluctuations.
Purpose of the Study:
- To investigate the molecular mechanisms of thermoadaptation in adenylate kinase catalysis.
- To understand how enzymes evolved to function across a wide range of temperatures over 3 billion years.
Main Methods:
- Ancestral sequence reconstruction of adenylate kinase spanning 3 billion years.
- Characterization of enzyme activity and stability across evolutionary timescales.
- Analysis of molecular mechanisms underlying catalytic speed and thermoadaptation.
Main Results:
- Evolutionary adaptation of adenylate kinase to cooler temperatures was achieved by exploiting transition-state heat capacity.
- Tracing enzyme evolution revealed active evolutionary pressures and refuted the activity/stability trade-off.
- Catalytic speed of adenylate kinase was identified as an evolutionary driver for organismal fitness.
Conclusions:
- Enzyme thermoadaptation is driven by exploiting thermodynamic properties like transition-state heat capacity.
- Evolutionary history of enzymes provides insights into molecular adaptation and organismal fitness.
- Adenylate kinase's catalytic speed is a key factor in its evolutionary success.
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