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Cysteine conjugate beta-lyase.

J Stevens, W B Jakoby

    Molecular Pharmacology
    |May 1, 1983
    PubMed
    Summary
    This summary is machine-generated.

    Rat liver cysteine conjugate beta-lyase, an enzyme in mercapturic acid synthesis, was purified. This enzyme catalyzes reactions with substrates containing nonpolar leaving groups, leading to suicide inhibition.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Drug Metabolism

    Background:

    • Mercapturic acid synthesis is a key pathway for xenobiotic detoxification.
    • Cysteine conjugate beta-lyase (CCB) plays a role in a shunt pathway of mercapturic acid synthesis.
    • Understanding CCB function is crucial for xenobiotic metabolism research.

    Purpose of the Study:

    • To purify and characterize cysteine conjugate beta-lyase from rat liver.
    • To investigate the substrate specificity and catalytic mechanism of CCB.
    • To elucidate the inhibitory mechanism of CCB activity.

    Main Methods:

    • Enzyme purification techniques were employed to isolate CCB from rat liver.
    • Enzyme activity assays were performed using various cysteine conjugate substrates.

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  • Kinetic studies were conducted to determine substrate specificity and inhibition patterns.

    • Main Results:

    • Purified rat liver CCB demonstrated activity with aromatic thioethers of cysteine and aliphatic amino acid derivatives.
    • Substrates like S-1,2-dichlorovinyl-L-cysteine and beta-chloroalanine were found to be active.
    • Catalysis by CCB resulted in time-dependent "suicide" inhibition with a partition ratio of approximately 600.

    Conclusions:

    • Rat liver CCB is an enzyme involved in mercapturic acid synthesis with broad substrate specificity.
    • The enzyme utilizes pyridoxal phosphate in its catalytic mechanism.
    • CCB undergoes self-inactivation during substrate catalysis, suggesting a mechanism for regulating its activity.