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Phosphofructokinase: structure and control.

P R Evans, G W Farrants, P J Hudson

    Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
    |June 26, 1981
    PubMed
    Summary
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    Bacillus stearothermophilus phosphofructokinase exhibits cooperative kinetics and allosteric regulation. Structural analysis reveals active and allosteric sites, explaining substrate binding and enzyme activation mechanisms.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Enzymology

    Background:

    • Phosphofructokinase (PFK) is a key glycolytic enzyme.
    • Bacillus stearothermophilus PFK displays cooperative kinetics and allosteric regulation by ADP and phosphoenolpyruvate.

    Purpose of the Study:

    • To elucidate the structural basis of PFK's cooperative kinetics and allosteric regulation.
    • To determine the active conformation of the enzyme and ligand-binding sites.

    Main Methods:

    • X-ray crystallography to solve the enzyme's structure at 2.4 A resolution.
    • Ligand-binding site identification and analysis.
    • Refinement of enzyme-ligand complexes (F6P, ADP, ATP).

    Main Results:

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  • The crystal structure of active PFK revealed three ligand-binding sites: two for substrates (F6P, ATP) and one for allosteric effectors (ADP, phosphoenolpyruvate).
  • The active site accommodates F6P and ATP, with ATP's gamma-phosphate positioned for phosphoryl transfer.
  • Substrate binding involves arginines from neighboring subunits, suggesting a mechanism for cooperativity. Allosteric activator ADP is also bound by residues from two subunits.

    • Conclusions:

    • The determined structure provides insights into the allosteric regulation and cooperative substrate binding of PFK.
    • Structural interactions explain how ADP activates and phosphoenolpyruvate inhibits the enzyme.
    • The findings contribute to understanding enzyme mechanisms and allosteric control in glycolysis.