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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Evolutionary aspects of enzyme dynamics.

Judith P Klinman1, Amnon Kohen2

  • 1Department of Chemistry, Department of Molecular and Cell Biology, and the California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, California 94720 and.

The Journal of Biological Chemistry
|September 12, 2014
PubMed
Summary
This summary is machine-generated.

Evolutionary pressure shapes enzyme function by influencing protein dynamics, not just chemistry. Studies on dihydrofolate reductases and alcohol dehydrogenases reveal how protein flexibility aids adaptation to different environments.

Keywords:
Alcohol Dehydrogenase (ADH)EnzymeEnzyme CatalysisEnzyme KineticsEnzyme MechanismEnzyme MutationEvolutionFolate MetabolismMolecular EvolutionProtein Evolution

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Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Structural Biology

Background:

  • Enzyme catalysis is central to biological processes, but the role of evolutionary pressure on the chemical step remains unclear, especially as chemistry is often not rate-limiting in optimized systems.
  • Understanding enzyme evolution requires linking structural changes to functional adaptations.

Purpose of the Study:

  • To investigate the evolutionary relationship between protein dynamics and the chemical step in enzyme catalysis.
  • To explore molecular details of convergent and divergent evolution in enzyme families.
  • To determine if protein dynamics contribute to enzyme adaptation under varying physiological conditions.

Main Methods:

  • Utilized a multidisciplinary approach combining kinetics, kinetic isotope effects, molecular biology, biophysics, and bioinformatics.
  • Examined two enzyme families: dihydrofolate reductases and alcohol dehydrogenases.
  • Analyzed evolutionary changes in protein structure and dynamics.

Main Results:

  • Provided insights into the molecular mechanisms of both convergent and divergent evolution in enzymes.
  • Demonstrated that protein dynamics across the entire enzyme structure can be crucial for adaptation.
  • Linked evolutionary alterations in enzymes to specific vibrational and conformational states.

Conclusions:

  • Protein dynamics play a significant role in enzyme adaptation to diverse physiological conditions.
  • Evolutionary changes in enzymes are connected to their dynamic properties, influencing catalytic efficiency.
  • Integrated approaches are effective for understanding the interplay between enzyme evolution, dynamics, and function.