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[Monkey liver microsomal glucose-6-phosphatase].

J P Benedetto, M B Martel, R Got

    Biochimie
    |January 1, 1979
    PubMed
    Summary
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    Glucose-6-phosphatase exhibits dual roles as a phosphohydrolase and phosphotransferase. Kinetic analysis reveals its substrate specificity and inhibition patterns, highlighting its multifunctional nature in enzymatic reactions.

    Area of Science:

    • Enzymology
    • Biochemistry
    • Molecular Biology

    Background:

    • Glucose-6-phosphatase is a key enzyme in glucose metabolism.
    • Its precise kinetic properties and substrate range require further elucidation.

    Purpose of the Study:

    • To kinetically characterize glucose-6-phosphatase.
    • To investigate its phosphohydrolase and phosphotransferase activities.
    • To determine substrate affinities, inhibition mechanisms, and reaction kinetics.

    Main Methods:

    • Enzyme kinetics assays were performed.
    • Substrate specificity was tested using various phosphate donors and acceptors.
    • Inhibition patterns were analyzed using different inhibitors.
    • Kinetic parameters (Km, Ki, Vmax) were determined.

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    Main Results:

    • The enzyme displayed higher affinity for glucose-6-phosphate (Km = 2.5 mM) than mannose-6-phosphate.
    • Carbamylphosphate served as a phosphoryl donor with D-glucose as an acceptor, indicating phosphotransferase activity.
    • Mixed-type inhibition was observed with beta-glycerophosphate and D-glucose, while pyrophosphate acted as a non-competitive inhibitor.
    • Detergents did not affect enzyme activity, and no latency was observed.

    Conclusions:

    • Glucose-6-phosphatase is a multifunctional enzyme with distinct phosphohydrolase and phosphotransferase activities.
    • Its kinetic properties are well-defined, providing insights into its catalytic mechanisms.
    • The enzyme's stability in the presence of detergents suggests its potential for various applications.