Llorente N, de Castro I N
Rev Esp Fisiol. 1977 Jun;33(2):135-42.
The activity of NAD+ and NADP+-linked aldehyde dehydrogenases has been investigated in yeast cells grown under different conditions. As occurs in other dehydrogenase reactions the NAD(P)+-linked enzyme was strongly repressed in all hypoxic conditions; nervetheless, the NADP+-linked enzyme was active. The results suggest that the NAD(P)+ aldehyde dehydrogenase is involved in the oxidation of ethanol to acetyl-CoA, and that when the pyruvate dehydrogenase complex is repressed the NADP+-linked aldehyde dehydrogenase is operative as an alternative pathway from pyruvate to acetyl-CoA: pyruvate leads to acetaldehyde leads to acetate leads to acetyl-Coa. In these conditions the supply of NADPH is advantageous to the cellular economy for biosynthetic purposes. Short term adaptation experiments suggest that the regulation of the levels of the aldehyde dehydrogenase-NAD(P)+ takes place by the de novo synthesis of the enzyme.
在不同条件下生长的酵母细胞中，对NAD⁺和NADP⁺连接的醛脱氢酶的活性进行了研究。正如在其他脱氢酶反应中一样，NAD(P)⁺连接的酶在所有缺氧条件下均受到强烈抑制；然而，NADP⁺连接的酶是有活性的。结果表明，NAD(P)⁺醛脱氢酶参与乙醇氧化为乙酰辅酶A的过程，并且当丙酮酸脱氢酶复合体受到抑制时，NADP⁺连接的醛脱氢酶作为从丙酮酸到乙酰辅酶A的替代途径发挥作用：丙酮酸生成乙醛，乙醛生成乙酸，乙酸生成乙酰辅酶A。在这些条件下，NADPH的供应对细胞用于生物合成目的的代谢过程有利。短期适应性实验表明，醛脱氢酶-NAD(P)⁺水平的调节是通过该酶的从头合成进行的。
