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Revisiting some Observations Related to the High Pressure Action on Enzyme Reactions

  • M. J. Kornblatt
  • J. A. Kornblatt
  • C. Balny
Conference paper

Abstract

An enzyme or ribozyme catalyzes the conversion of a chemical (substrate) into another chemical (product). In order to do this, the macromolecule must interact with the substrate and product, as well with the environment. The enzyme or ribozyme exists in a dynamic equilibrium between multiple conformational states. The environment — temperature, pressure, salt, cosolvent, pH, etc. — selects the set point for equilibrium. It is necessary to point out that not all conformations will be catalytically active but that they can interconvert with species that are. This means that by a judicious choice of perturbant—for example, pressure at “constant” T, pH, ionic strength, cosolvent .... — we can interrogate both catalytically active and inactive species. We do the same for T at “constant” P, ..... Reaction rates then give us information on how the system responds globally to the perturbant. If this can be combined with independent information on the effects of perturbant on structural equilibria of the enzyme and the effects of perturbants on the chemistry of the process (vide infra) we stand a good chance having a complete structural and mechanistic interpretation of a biochemical process. This is the goal of the work carried out in our laboratory.

Keywords

Creatine Kinase Reversed Micelle Elementary Step Guanidine Hydrochloride Creatine Kinase Reaction 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 2003

Authors and Affiliations

  • M. J. Kornblatt
    • 1
    • 2
  • J. A. Kornblatt
    • 1
    • 2
  • C. Balny
    • 2
  1. 1.Enzyme Research Group, Dept of BiologyConcordia UniversityMontrealCanada
  2. 2.INSERM U128, IFR 24CNRSMontpellier Cedex 5France

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