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Related Experiment Videos

[Substrate specificity of soluble mitochondrial ATPase].

I A Kozlov, V A Metel'sakaia, S N Mikhaĭlov

    Biokhimiia (Moscow, Russia)
    |January 1, 1978
    PubMed
    Summary

    Mitochondrial ATPase hydrolyzes ATP and analogs, with varying Vmax and similar Km values. Certain analogs inhibit the enzyme by binding in a tense conformation, suggesting a specific substrate interaction mechanism.

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    Comparative Analysis of the Biosynthesis of Isoprenoid and Aromatic Cytokinins.

    Doklady. Biochemistry and biophysics·2019

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Mitochondrial ATPase is crucial for cellular energy production.
    • Understanding its substrate specificity is key to elucidating mitochondrial function.

    Purpose of the Study:

    • To determine the kinetic parameters of soluble mitochondrial ATPase for ATP and various analogs.
    • To investigate the binding and hydrolysis mechanisms of modified ATP substrates.

    Main Methods:

    • Enzyme kinetics assays (Vmax, Km) were performed.
    • Hydrolysis rates of ATP analogs were measured.
    • Inhibition constants (Ki) were determined for non-hydrolyzable analogs.

    Main Results:

    • Vmax decreased in the order: 2'-deoxy-ATP > ATP > etheno-ATP > GTP > 3'-O-methylATP > UTP.

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  • ATP, 2'-deoxy-ATP, 3'-O-methyl-ATP, GTP, and etheno-ATP showed similar apparent Km values.
  • CTP was neither hydrolyzed nor inhibitory.
  • Open-ribose cycle nucleoside triphosphate derivatives and hydrocarbon radical-containing analogs acted as effective inhibitors.

    • Conclusions:

    • Mitochondrial ATPase exhibits specific substrate preferences.
    • Inhibitory analogs suggest binding occurs in a tense conformation within the active site.
    • This conformational binding likely precedes substrate hydrolysis.