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 γ1γ1 >γ2γ2 ∼ αα >ππ ∼ β2β2 ∼ β1β1 ⪢ χχ; kcatKm values are 1.4 × 108, 1.9 × 107, 1.4 × 107, 5.6 × 106, 1.6 × 106 and 2.5 × 103 M−1min−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 leels among and within various populations.
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