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Human GMP synthetase.

T Page, B Bakay, W L Nyhan

    The International Journal of Biochemistry
    |January 1, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Human GMP synthetase activity is highest in skin fibroblasts. This enzyme, crucial for purine biosynthesis, was purified and characterized, revealing specific kinetic properties and inhibition patterns.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Human Physiology

    Background:

    • Guanosine monophosphate (GMP) synthetase is a key enzyme in the de novo purine biosynthesis pathway.
    • Understanding human GMP synthetase is essential for metabolic research and potential therapeutic interventions.

    Purpose of the Study:

    • To determine the tissue distribution of GMP synthetase activity in human tissues.
    • To purify and biochemically characterize human GMP synthetase from cultured skin fibroblasts.
    • To compare the properties of human GMP synthetase with those from other species.

    Main Methods:

    • Enzyme activity assays were performed on various human tissue homogenates.
    • GMP synthetase was purified from cultured skin fibroblasts using ammonium sulfate fractionation and gel filtration.

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  • Kinetic parameters (Km values) for substrates (XMP, ATP, glutamine) were determined.
  • Inhibition studies were conducted using various compounds.

    • Main Results:

    • GMP synthetase activity was highest in cultured skin fibroblasts, followed by bone marrow, leukocytes, erythrocytes, placenta, and liver.
    • The enzyme was purified approximately 50-fold.
    • Km values were determined as 4.9 microM for XMP, 270 microM for ATP, and 340 microM for glutamine.
    • Ammonium sulfate could substitute for glutamine but was less efficient; ATP was the specific energy source.
    • Human GMP synthetase does not require reduced sulfhydryl compounds, unlike the calf thymus enzyme.
    • The enzyme is inhibited by ATP, dATP, azaserine, and hydroxylamine.

    Conclusions:

    • Human GMP synthetase exhibits distinct tissue distribution with highest activity in fibroblasts.
    • The purified human enzyme possesses specific substrate affinities and energy requirements.
    • Key differences exist between human and calf thymus GMP synthetase, particularly regarding sulfhydryl compound dependence.
    • The identified inhibitors provide insights into enzyme regulation and potential drug targets.