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Amine N-methyltransferases from rabbit liver.

S S Ansher, W B Jakoby

    The Journal of Biological Chemistry
    |March 25, 1986
    PubMed
    Summary

    Rabbit liver contains two N-methyltransferases that catalyze N-methylation of amines. These enzymes exhibit broad substrate specificity and share common properties, despite differences in isoelectric points.

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    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • N-methylation of amines is a crucial biological process.
    • Previously, distinct enzymes like amine N-methyltransferase, indolethylamine N-methyltransferase, and arylamine N-methyltransferase were thought to be responsible for these reactions.

    Purpose of the Study:

    • To investigate the enzymatic basis of N-methylation of amines in rabbit liver.
    • To characterize the enzymes responsible for these N-methylation activities.

    Main Methods:

    • Enzyme purification and characterization from rabbit liver.
    • Assays for N-methyltransferase activity using various amine substrates.
    • Immunological cross-reactivity studies using antibodies against the purified enzymes.
    • Determination of molecular mass and isoelectric points.

    Main Results:

    • Two related N-methyltransferase enzymes in rabbit liver accomplish the N-methylation activities previously ascribed to multiple enzymes.
    • Both enzymes demonstrate a broad and overlapping substrate specificity for primary and secondary amines.
    • The two enzymes share a molecular mass of 30,000 daltons and are immunologically related.
    • Despite similarities, the enzymes possess distinct isoelectric points.

    Conclusions:

    • Rabbit liver possesses two N-methyltransferases with broad substrate specificity that collectively account for various amine N-methylation reactions.
    • These enzymes are closely related, sharing molecular mass and immunological identity, but differ in isoelectric points, suggesting distinct molecular forms.

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