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Updated: Aug 8, 2026

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Kinetics of suicide substrates

S G Waley

    The Biochemical Journal
    |March 1, 1980
    PubMed

    Insights

    Enzyme inactivation by suicide substrates occurs alongside product formation during catalysis. New equations describe these concurrent processes, applicable when using catalytic enzyme quantities.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Chemical Kinetics

    Background:

    • Enzyme inactivation by suicide substrates is a critical process in biochemistry.
    • Understanding concurrent product formation and enzyme inactivation is essential for kinetic analysis.

    Purpose of the Study:

    • To derive and integrate equations for enzyme inactivation rates.
    • To describe the progress curves resulting from concurrent catalysis and inactivation.

    Main Methods:

    • Application of the steady-state hypothesis for catalytic enzyme quantities.
    • Derivation of inactivation rate equations.
    • Integration of derived equations to model progress curves.

    Main Results:

    • Concurrent formation of product and inactivation of enzyme during catalysis.
    • Development of integrated equations to describe progress curves.
    • Demonstration of the applicability of the steady-state hypothesis.

    Conclusions:

    • The derived equations accurately describe enzyme inactivation progress curves.
    • The study provides a mathematical framework for analyzing suicide substrate kinetics.
    • This work is relevant for understanding enzyme mechanisms and drug development.

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