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Related Experiment Videos

Interaction between D-amino acid oxidase and small molecules.

K Horiike, K Shiga, A Isomoto

    Journal of Biochemistry
    |November 1, 1976
    PubMed
    Summary

    p-aminobenzoate binds to hog kidney D-amino acid oxidase, favoring dimer formation. This binding enhances enzyme affinity and stabilizes the dimer structure, with distinct binding sites for the substrate and intersubunit interactions.

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    Area of Science:

    • Biochemistry
    • Enzyme kinetics
    • Protein-ligand interactions

    Background:

    • Hog kidney D-amino acid oxidase exists in monomer-dimer equilibrium.
    • Understanding enzyme-ligand interactions is crucial for enzyme mechanism studies.

    Purpose of the Study:

    • To investigate the effect of pH on p-aminobenzoate binding to D-amino acid oxidase monomers and dimers.
    • To elucidate the binding stoichiometry, affinity, and cooperativity of p-aminobenzoate interaction with the enzyme.

    Main Methods:

    • Kinetic methods
    • Spectrophotometric titration
    • Analysis of pH dependence of inhibitor binding

    Main Results:

    • p-Aminobenzoate binds to the dimer with a maximum of two molecules, exhibiting no cooperativity between active sites.
    • The dimer shows significantly higher affinity for p-aminobenzoate than the monomer across pH 6.5-10.
    • p-Aminobenzoate binding induces dimerization and stabilizes the dimer interaction energy by 1-2 kcal/mole.
    • Binding sites for p-aminobenzoate and intersubunit interactions are distinct, as evidenced by p-aminobenzoate-induced dimerization.

    Conclusions:

    • p-Aminobenzoate acts as an inducer of dimerization for D-amino acid oxidase.
    • The enzyme-inhibitor interaction involves ionizing groups with a pK of approximately 8.7, without cooperativity between dimer subunits.
    • The study clarifies the complex interplay between pH, ligand binding, and quaternary structure in D-amino acid oxidase.

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