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    Biochem Biophys Res Commun. 1991 Jan 31;174(2):701-7.

    Human liver alcohol dehydrogenases catalyze the oxidation of the intermediary alcohols of the shunt pathway of mevalonate metabolism.

    Keung WM.

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    Center for Biochemical and Biophysical Sciences and Medicine, Harvard Medical School, Boston, Massachusetts.

    Abstract

    Human liver alcohol dehydrogenase (ADH) catalyzes the oxidation of 3,3-dimethylallyl alcohol, the intermediary alcohol of the shunt pathway of mevalonate metabolism. ADH isozymes differ in their activities toward this alcohol in the order gamma 1 gamma 1 greater than gamma 2 gamma 2 approximately alfa alfa greater pi pi approximately beta 2 beta 2 approximately beta 1 beta 1 much greater than chi chi; kcat/Km values are 1.4 x 10(8), 1.9 x 10(7), 1.4 x 10(7), 5.6 x 10(6), 3.6 x 10(6), 1.6 x 10(6) and 2.5 x 10(3) M-1 min-1, respectively. The intermediary alcohols geraniol and farnesol of the proposed branch pathways of mevalonate metabolism are also oxidized by these isozymes with similar relative efficiencies. The genetic determinants of ADH isozymes may contribute to the observed differences in serum cholesterol levels among and within various populations.

    PMID:
    1993065
    [PubMed - indexed for MEDLINE]

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