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Deviation from Michaelis-Menten kinetics for fumarase

M J Crabbe, W G Bardsley

    The Biochemical Journal
    |August 1, 1976
    PubMed
    Summary
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    Fumarase enzyme kinetics show complex behavior at high malate concentrations, suggesting previously overlooked co-operative effects or a mix of isoenzymes. This study provides new insights into enzyme mechanisms.

    Area of Science:

    • Biochemistry
    • Enzyme kinetics

    Background:

    • Fumarase catalyzes the reversible hydration of fumarate to L-malate.
    • Understanding enzyme kinetics is crucial for elucidating biological mechanisms.

    Purpose of the Study:

    • To investigate the steady-state kinetics of fumarase.
    • To analyze enzyme behavior over an extended substrate concentration range.

    Main Methods:

    • Employed novel analytical methods for kinetic studies.
    • Performed experiments at pH 7.0 with varying malate concentrations up to 100 mM.

    Main Results:

    • An initial-rate equation of at least fourth degree for malate was determined.
    • No significant dead-end complex formation was observed.

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  • Complex kinetic behavior was noted in the absence of enzyme aggregation.

    • Conclusions:

    • The observed kinetics suggest potential co-operative effects in fumarase.
    • A mixture of isoenzymes with complex individual kinetics may also contribute.
    • These findings challenge previous assumptions about fumarase mechanisms.