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Reaction intermediate analogues for enolase.

V E Anderson, P M Weiss, W W Cleland

    Biochemistry
    |June 5, 1984
    PubMed
    Summary
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    Novel phosphonate compounds effectively inhibit yeast enolase by mimicking a key intermediate. These findings support a carbanion mechanism and highlight the role of Mg2+ coordination in enzyme inhibition.

    Area of Science:

    • Biochemistry
    • Enzyme kinetics
    • Medicinal chemistry

    Background:

    • Yeast enolase catalyzes the interconversion of 2-phosphoglycerate and phosphoenolpyruvate.
    • Understanding enolase's mechanism is crucial for developing targeted inhibitors.

    Purpose of the Study:

    • To investigate the inhibitory potential of novel aci-form carbanion analogues against yeast enolase.
    • To elucidate the mechanism of enolase inhibition and the role of specific functional groups.

    Main Methods:

    • Synthesis and characterization of phosphonate-based compounds.
    • Enzyme inhibition assays measuring inhibition constants (Ki) in the presence of Mg2+.
    • Analysis of binding kinetics, including slow-binding inhibition.

    Main Results:

    Related Experiment Videos

    • Several analogues, including (3-hydroxy-2-nitropropyl)phosphonate and phosphonoacetohydroxamate, showed potent inhibition with Ki values in the nanomolar to picomolar range.
    • Compounds with a negatively charged metal ligand at the C-3 position analogue demonstrated stronger binding than those with a nitro group.
    • Inhibitors I, IV, VI, and VII exhibited slow-binding kinetics.

    Conclusions:

    • The study supports a carbanion mechanism for yeast enolase.
    • The 3-hydroxyl group of 2-phosphoglycerate likely coordinates with Mg2+ during the enzymatic reaction.
    • The findings provide insights for designing more effective enolase inhibitors.