人胞质醛脱氢酶的视网膜氧化活性及其生物学作用。

Enzyme Pub Date : 1992-01-01 DOI:10.1159/000468794
A Yoshida, L C Hsu, V Davé
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引用次数: 160

摘要

主要的细胞质醛脱氢酶同工酶(ALDH1)对视网膜氧化为视黄酸具有较强的活性,而主要的线粒体ALDH2和胃细胞质ALDH3则没有这种活性。在pH为7.5时,ALDH1对视网膜的催化Km约为0.06 μ mol/l,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,在低浓度(< 0.01 μ mol/l)视网膜组织中,ALDH1能有效地从视网膜生成视黄酸。ALDH1基因有激素反应元件。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。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Retinal oxidation activity and biological role of human cytosolic aldehyde dehydrogenase.

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.

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