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6-Phosphogluconate dehydrogenase. Purification and kinetics.

M L Toews, M I Kanji, W R Carper

    The Journal of Biological Chemistry
    |November 25, 1976
    PubMed
    Summary
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    This study details the purification of pig liver 6-phosphogluconate dehydrogenase. The enzyme, located in the cytoplasm, has a molecular weight of 83,000 and follows a sequential reaction mechanism.

    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • 6-phosphogluconate dehydrogenase is a key enzyme in the pentose phosphate pathway.
    • Understanding its properties is crucial for metabolic studies.

    Purpose of the Study:

    • To isolate and purify 6-phosphogluconate dehydrogenase from pig liver.
    • To characterize its biochemical and kinetic properties.

    Main Methods:

    • Enzyme purification techniques.
    • Gel electrophoresis for molecular weight determination.
    • Enzyme kinetics assays.
    • Cellular fractionation.

    Main Results:

    • Purified 6-phosphogluconate dehydrogenase with estimated molecular weight of 83,000 (subunits 42,000).

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  • Optimal activity at pH 8.5; Mg2+ not required, inhibitory above 20 mM.
  • Enzyme localized in the soluble cytoplasm.
  • Sequential reaction mechanism with NADP+ binding first.
  • Michaelis constant for 6-phosphogluconate: 13.5 μM.
  • Dissociation constants for NADP+ (4.8 μM) and NADPH (5.1 μM).

    • Conclusions:

    • The study successfully isolated and characterized pig liver 6-phosphogluconate dehydrogenase.
    • Kinetic data supports a sequential binding mechanism.
    • Enzyme properties provide insights into its role in cellular metabolism.