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Validity of transfer-function representation of input-output relation in allosteric models.

N Sakamoto, T Naka

    Bio Systems
    |January 1, 1986
    PubMed
    Summary

    A new transfer-function model approximates allosteric enzyme responses near steady state. This method accurately describes Koshland-Nemethy-Filmer and Monod-Wyman-Changeux models under specific conditions, aiding metabolic pathway analysis.

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    Area of Science:

    • Biochemistry
    • Chemical Engineering
    • Systems Biology

    Background:

    • Allosteric enzymes exhibit complex kinetics crucial for metabolic regulation.
    • Accurate modeling of enzyme dynamics is essential for understanding cellular processes.
    • Existing models may not fully capture transient responses around steady states.

    Purpose of the Study:

    • To develop an analytical transfer-function representation for allosteric enzyme reaction velocity.
    • To approximate the input-output response of allosteric enzymes near a steady state.
    • To assess the validity of this representation for different allosteric models and kinetic parameters.

    Main Methods:

    • Derived a transfer-function representation assuming exponential changes in reaction velocity.

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  • Examined the Koshland-Nemethy-Filmer (KNF) and Monod-Wyman-Changeux (MWC) dimeric models.
  • Compared the transfer-function approximation with exact responses from numerical simulations of rate equations.

    • Main Results:

    • The transfer-function representation is valid in a wider region with decreasing influx rate.
    • For the KNF model, the representation is valid for negative cooperativity but not positive cooperativity.
    • For the MWC model, validity decreases with increasing cooperativity.

    Conclusions:

    • The developed transfer-function representation offers an approximate analytical description of allosteric enzyme kinetics.
    • The model's validity is dependent on the specific allosteric model, cooperativity, and influx rate.
    • This approach can be extended to model complex metabolic pathways involving Michaelis-Menten and allosteric reactions.