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Modulating Enzyme Activity by Altering Protein Dynamics with Solvent.

Michael R Duff1, Jose M Borreguero2, Matthew J Cuneo3

  • 1Biochemistry & Cellular and Molecular Biology Department , University of Tennessee , Knoxville , Tennessee , United States.

Biochemistry
|June 15, 2018
PubMed
Summary
This summary is machine-generated.

Altering enzyme dynamics using organic solvents can control enzyme activity. Suppressing motions in dihydrofolate reductase (DHFR) with isopropanol decreased its hydride transfer rate, demonstrating a link between dynamics and catalysis.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Enzyme activity is influenced by structure and dynamics, but the role of dynamics is debated.
  • Controlling enzyme dynamics offers a novel way to modulate enzyme function.

Purpose of the Study:

  • To investigate the impact of altered enzyme dynamics on catalytic activity.
  • To explore the use of aqueous organic solvent mixtures to control enzyme dynamics.

Main Methods:

  • Utilized aqueous mixtures of isopropanol (IPA) to modify enzyme dynamics.
  • Employed stopped-flow kinetics to measure reaction rates.
  • Used X-ray crystallography and quasi-elastic neutron scattering to analyze enzyme structure and dynamics.

Main Results:

  • A 2.2-fold decrease in the hydride transfer rate (khydride) of dihydrofolate reductase (DHFR) was observed at 20% IPA.
  • No significant changes in enzyme structure were detected via X-ray crystallography.
  • Quasi-elastic neutron scattering confirmed suppressed enzyme motions in the mixed solvent.

Conclusions:

  • Enzyme dynamics can be modulated by aqueous organic solvents to control enzyme activity.
  • Suppressed dynamics in DHFR lead to reduced catalytic efficiency by limiting access to functional conformational substates.
  • This approach offers insights into rate-limiting dynamics in catalysis and has implications for enzyme engineering.