Human cytochrome P-450 PB-I: A multigene family involved in mephenytoin and steroid oxidations that maps to chromosome 10

R. R. Meehan, J. R. Gosden, D. Rout, N. D. Hastie, T. Friedberg, M. Adesnik, R. Buckland, V. Van Heyningen, J. Fletcher, N. K. Spurr, J. Sweeney, C. R. Wolf

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    86 Citations (Scopus)

    Abstract

    The cytochrome P-450 monooxygenase system possesses catalytic activity toward many exogenous compounds (e.g., drugs, insecticides, and polycyclic aromatic hydrocarbons) and endogenous compounds (e.g., steroids, fatty acids, and prostaglandins). Multiple forms of cytochrome P-450 with different substrate specificities have been isolated. In the presence paper we report the isolation and sequence of a cDNA clone for the human hepatic cytochrome P-450 responsible for mephenytoin (an anticonvulsant) oxidation. The mephenytoin cytochrome P-450 is analogous to the rat cytochrome P-450 termed PB-1 (family P450C2C). We also report that human PB-1 is encoded by one of a small family of related genes all of which map to human chromosome 10q24.1-10q24.3. The endogenous role of this enzyme appears to be in steroid oxidations. This cytochrome P-450 family does not correspond to any of the hepatic cytochrome P-450 gene families previously mapped in humans.

    Original languageEnglish
    Pages (from-to)26-37
    Number of pages12
    JournalAmerican Journal of Human Genetics
    Volume42
    Issue number1
    Publication statusPublished - 1988

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