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Liver microsomal epoxide hydrase.

A Y Lu, D M Jerina, W Levin

    The Journal of Biological Chemistry
    |June 10, 1977
    PubMed
    Summary
    This summary is machine-generated.

    This study investigated epoxide hydrase activity in rat liver microsomes. Purified epoxide hydrase showed altered kinetics and substrate affinity influenced by lipid concentration, suggesting substrate partitioning in micelles.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Pharmacology

    Background:

    • Epoxide hydrase (EH) is crucial for metabolizing xenobiotics.
    • Understanding EH substrate specificity and kinetics is vital for drug metabolism studies.
    • Rat liver microsomes are a common source for studying EH activity.

    Purpose of the Study:

    • To determine the substrate specificity of membrane-bound and purified rat liver epoxide hydrase.
    • To investigate the kinetic differences between membrane-bound and purified EH.
    • To elucidate the role of lipids in EH activity and substrate kinetics.

    Main Methods:

    • Enzyme assays using various alkene and arene oxides.
    • Kinetic analysis of purified epoxide hydrase with and without lipid supplementation.

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  • Determination of apparent Km values under varying enzyme and lipid concentrations.

    • Main Results:

    • Both membrane-bound and purified EH hydrated alkene and arene oxides.
    • Purified EH exhibited shorter linearity of reaction rates compared to membrane-bound EH.
    • Apparent Km values were dependent on lipid concentration for purified EH, suggesting substrate partitioning.

    Conclusions:

    • Lipid environment significantly influences the kinetic parameters of purified epoxide hydrase.
    • The observed Km dependency on lipid concentration is consistent with a model of substrate partitioning between micelles and aqueous phases.
    • These findings highlight the importance of considering lipid interactions in EH studies.