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Amine N-sulfotransferase.

S G Ramaswamy, W B Jakoby

    The Journal of Biological Chemistry
    |July 25, 1987
    PubMed
    Summary
    This summary is machine-generated.

    Researchers purified a guinea pig liver enzyme, amine N-sulfotransferase, which transfers sulfuryl groups to various amines, forming sulfamates. This enzyme

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Drug Metabolism

    Background:

    • Amine N-sulfotransferases are crucial enzymes involved in the metabolism of various compounds.
    • Understanding the substrate specificity and catalytic mechanisms of these enzymes is vital for drug development and toxicology.

    Purpose of the Study:

    • To isolate and characterize a highly purified amine N-sulfotransferase from guinea pig liver.
    • To investigate the substrate specificity and potential O-sulfotransferase activity of the purified enzyme.

    Main Methods:

    • Purification of amine N-sulfotransferase from guinea pig liver.
    • Enzyme assays to determine catalytic activity with various amine substrates.
    • Analysis of reaction products using appropriate biochemical techniques.

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    Main Results:

    • A highly purified amine N-sulfotransferase was successfully isolated from guinea pig liver.
    • The enzyme demonstrated broad substrate specificity, accepting a wide range of primary and secondary amines, including aniline, 2-naphthylamine, octylamine, tetrahydroisoquinoline, desmethylimipramine, and cyclohexylamine.
    • Cyclohexylamine was converted to cyclamate, a sugar substitute.
    • Enzyme activity was dependent on the presence of an unprotonated amino group.
    • The purified enzyme exhibited O-sulfotransferase activities, indicating potential dual functionality.

    Conclusions:

    • The purified guinea pig liver amine N-sulfotransferase is a versatile enzyme with broad substrate acceptance.
    • The enzyme's ability to accept diverse amines suggests its significant role in xenobiotic metabolism.
    • The observed O-sulfotransferase activity implies that oxygen transfer might be an intrinsic function of this N-sulfotransferase.