Keung W M
Center for Biochemical and Biophysical Sciences and Medicine, Harvard Medical School, Boston, Massachusetts.
Biochem Biophys Res Commun. 1991 Jan 31;174(2):701-7. doi: 10.1016/0006-291x(91)91474-q.
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.
人肝脏乙醇脱氢酶（ADH）催化甲羟戊酸代谢旁路途径的中间醇3,3 - 二甲基烯丙醇的氧化。ADH同工酶对这种醇的活性顺序为γ1γ1大于γ2γ2约等于αα大于ππ约等于β2β2约等于β1β1远大于χχ；kcat/Km值分别为1.4×10⁸、1.9×10⁷、1.4×10⁷、5.6×10⁶、3.6×10⁶、1.6×10⁶和2.5×10³M⁻¹min⁻¹。甲羟戊酸代谢拟议分支途径的中间醇香叶醇和法呢醇也被这些同工酶以相似的相对效率氧化。ADH同工酶的遗传决定因素可能导致不同人群之间以及人群内部观察到的血清胆固醇水平差异。
