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Pyruvate kinase: activation by and catalytic role of the monovalent and divalent cations

T Nowak, C Suelter

    Molecular and Cellular Biochemistry
    |March 13, 1981
    PubMed

    Insights

    Pyruvate kinase activity is activated by both monovalent cations like potassium and divalent cations such as magnesium. Microbial enzymes show varied responses to monovalent cations, impacting catalytic mechanisms.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Molecular Biology

    Background:

    • Pyruvate kinase is a crucial enzyme in glycolysis.
    • Cation activators significantly influence enzyme kinetics and function.
    • Variations in pyruvate kinase structure and activation exist between species and even within microbial strains.

    Purpose of the Study:

    • To review the role of monovalent and divalent cations in pyruvate kinase activation.
    • To explore the differential activation of microbial pyruvate kinase forms.
    • To elucidate the catalytic mechanisms involving cation cofactors.

    Main Methods:

    • Review of existing literature on pyruvate kinase activation.
    • Analysis of Nuclear Magnetic Resonance (NMR) data regarding cation binding sites.
    • Examination of kinetic data for various pyruvate kinase preparations under different conditions.

    Main Results:

    • Vertebrate pyruvate kinase requires monovalent cations (e.g., K+) for catalysis.
    • Microbial pyruvate kinase exhibits varied responses to monovalent cations; E. coli produces two forms.
    • Divalent cations (Mg+2 optimal, but Co+2, Mn+2, Ni+2 also active) are essential, with evidence suggesting two moles are required per catalytic event.

    Conclusions:

    • Monovalent cations play a direct role in pyruvate kinase catalysis, binding near divalent cations.
    • The dual forms of E. coli pyruvate kinase highlight enzymatic adaptability.
    • While divalent cation requirement is established, their precise dual role in catalysis requires further investigation.

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