MacKerell A D, Blatter E E, Pietruszko R
Alcohol Clin Exp Res. 1986 Jun;10(3):266-70. doi: 10.1111/j.1530-0277.1986.tb05087.x.
Michaelis constants and maximal velocities for phenylacetaldehyde (a metabolite of phenylethylamine), 3,4-dihydroxyphenylacetaldehyde (a metabolite of dopamine), 5-hydroxyindole acetaldehyde (a metabolite of serotonin), and 3,4-dihydroxyphenylglycolaldehyde (a metabolite of epinephrine and norepinephrine) have been determined for both cytoplasmic (E1) and mitochondrial (E2) isozymes of human liver aldehyde dehydrogenase (EC 1.2.1.3). Kinetic constants with biogenic aldehydes have never been previously determined for individual homogeneous isozymes of aldehyde dehydrogenase from any species. Mathematical treatment of these constants suggests that competition with acetaldehyde during alcohol metabolism would severely inhibit dehydrogenation of biogenic aldehydes with the mitochondrial and not the cytoplasmic isozyme of human liver aldehyde dehydrogenase.
已测定人肝醛脱氢酶（EC 1.2.1.3）的细胞质（E1）和线粒体（E2）同工酶对苯乙醛（苯乙胺的一种代谢产物）、3,4 - 二羟基苯乙醛（多巴胺的一种代谢产物）、5 - 羟基吲哚乙醛（血清素的一种代谢产物）以及3,4 - 二羟基苯乙醇醛（肾上腺素和去甲肾上腺素的一种代谢产物）的米氏常数和最大反应速度。此前从未测定过来自任何物种的醛脱氢酶单个同质性同工酶与生物源性醛类的动力学常数。对这些常数的数学处理表明，在酒精代谢过程中与乙醛竞争会严重抑制人肝醛脱氢酶的线粒体同工酶而非细胞质同工酶对生物源性醛类的脱氢作用。
