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[Deviations from hyperbolic kinetics in slowly dissociating allosteric enzyme systems].

B I Kuranov, A I Dorozhko, Z S Kagan

    Biokhimiia (Moscow, Russia)
    |July 1, 1975
    PubMed
    Summary
    This summary is machine-generated.

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    Enzyme kinetics can be complex in slowly dissociating systems where oligomeric forms interconvert slowly. These systems exhibit intricate initial reaction rate plots against substrate or effector concentrations, showing varied behaviors.

    Area of Science:

    • Biochemistry
    • Enzyme kinetics
    • Biophysical chemistry

    Context:

    • Discusses the kinetic behavior of dissociating enzyme systems.
    • Focuses on systems where equilibrium between oligomeric forms is slow relative to the enzymatic process.
    • Considers enzyme systems of the type Np <=> P, where P is the enzyme oligomer and p is the subunit (N >= 2).

    Purpose:

    • To analyze the complex kinetic behaviors observed in slowly dissociating enzyme systems.
    • To illustrate how differences in allosteric interactions between active and allosteric sites in P and p forms influence reaction kinetics.
    • To characterize the shapes of initial reaction rate (v) versus substrate (S) or effector (F) concentration plots.

    Summary:

    • In slowly dissociating enzyme systems, initial reaction rate (v) versus substrate concentration ([S]0) plots can display complex features like intermediate plateaus, simultaneous maxima and minima, and sigmoidality followed by plateaus.

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  • Similarly, v versus effector concentration ([F]0) plots can exhibit intermediate plateaus.
  • These complex kinetic profiles arise from the slow interconversion of enzyme oligomeric states and differing allosteric interactions.

    • Impact:

    • Provides insights into the complex allosteric regulation of enzymes.
    • Helps in understanding enzyme mechanisms where oligomerization dynamics are significant.
    • Contributes to the theoretical framework of enzyme kinetics for complex systems.