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Microsomal reductive glycosidase.

N R Bachur, M Gee

    The Journal of Pharmacology and Experimental Therapeutics
    |June 1, 1976
    PubMed
    Summary
    This summary is machine-generated.

    A novel reductive glycosidase in rat liver microsomes cleaves anthracycline antibiotics. This enzyme

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Pharmacology

    Background:

    • Anthracycline antibiotics are crucial in cancer therapy.
    • Understanding their metabolism is vital for optimizing treatment.
    • Microsomal enzymes play a significant role in drug metabolism.

    Purpose of the Study:

    • To identify and characterize a reductive glycosidase in rat liver microsomes.
    • To investigate the enzyme's activity on anthracycline antibiotics.
    • To elucidate the enzyme's properties and potential biological role.

    Main Methods:

    • Enzyme assays using rat liver microsomes.
    • Substrate incubation with anthracycline antibiotics (adriamycin, daunorubicin).
    • Analysis of reaction products (deoxyaglycones).

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  • Enzyme inhibition studies with oxygen, carbon monoxide, and other reagents.

    • Main Results:

    • A phenobarbital-inducible, NADPH-dependent reductive glycosidase was identified.
    • The enzyme efficiently cleaved adriamycin and daunorubicin to deoxyaglycones.
    • Optimal activity occurred at pH 7-7.4, with no metal requirements.
    • The enzyme was strongly inhibited by molecular oxygen (>95% at 20% O2).
    • It showed sensitivity to Cu++ and Zn++ but not CO, SKF 525A, or sulfhydryl reagents.
    • Activity was also detected in rat brain, kidney, and other tissues.

    Conclusions:

    • Rat liver microsomes possess a reductive glycosidase capable of metabolizing anthracyclines.
    • The enzyme's oxygen sensitivity suggests a potential in vivo regulatory role.
    • Further research into this enzyme could impact anthracycline drug development and application.