Yoshida A, Hsu L C, Davé V
Department of Biochemical Genetics, Beckman Research Institute of the City of Hope, Duarte, Calif.
Enzyme. 1992;46(4-5):239-44. doi: 10.1159/000468794.
The major cytosolic aldehyde dehydrogenase isozyme (ALDH1) exhibits strong activity for oxidation of retinal to retinoic acid, while the major mitochondrial ALDH2 and the stomach cytosolic ALDH3 have no such activity. The Km of ALDH1 for retinal is about 0.06 mumol/l at pH 7.5, and the catalytic efficiency (Vmax/Km) for retinal is about 600 times higher than that for acetaldehyde. Thus, ALDH1 can efficiently produce retinoic acid from retinal in tissues with low retinal concentrations (< 0.01 mumol/l). The gene for ALDH1 has hormone response elements. These findings suggest that the major physiological substrate of human ALDH1 is retinal, and that its primary biological role is generation of retinoic acid resulting in modulation of cell differentiation including hormone-mediated development.
主要的胞质醛脱氢酶同工酶（ALDH1）对视网膜氧化为视黄酸具有很强的活性，而主要的线粒体ALDH2和胃胞质ALDH3则没有这种活性。在pH 7.5时，ALDH1对视网膜的Km约为0.06 μmol/L，其对视网膜的催化效率（Vmax/Km）比对乙醛的催化效率高约600倍。因此，ALDH1能够在视网膜浓度较低（<0.01 μmol/L）的组织中有效地从视网膜产生视黄酸。ALDH1基因具有激素反应元件。这些发现表明，人类ALDH1的主要生理底物是视网膜，其主要生物学作用是产生视黄酸，从而调节细胞分化，包括激素介导的发育。
