Sawada H, Hara A, Nakayama T, Nakagawa M, Inoue Y, Hasebe K, Zhang Y P
Department of Biochemistry, Gifu Pharmaceutical University, Japan.
Biochem Pharmacol. 1988 Feb 1;37(3):453-8. doi: 10.1016/0006-2952(88)90214-6.
A major and a minor form of dihydrodiol dehydrogenase were co-purified with 17 beta-hydroxysteroid dehydrogenase and aldehyde reductase, respectively, to apparent homogeneity from liver cytosol of male ddY mice. The activities of dihydrodiol dehydrogenase and testosterone dehydrogenase or aldehyde reductase of the two enzyme forms comigrated electrophoretically. The major form of the enzyme oxidized 17 beta-hydroxysteroids and nonsteroidal alicyclic alcohols and reduced 17-ketosteroids and various synthetic carbonyl compounds, showing higher affinity for steroids than for xenobiotics. The activity of this enzyme form toward benzene dihydrodiol and testosterone exhibited identical thermostability and susceptibility to inhibition by quercitrin, SH-reagents, nonsteroidal estrogens and anti-inflammatory agents. On the other hand, the minor form of the enzyme, which oxidized benzene dihydrodiol but not 17 beta-hydroxysteroids, also reduced various aldehydes well and was specifically inhibited by barbiturates and sorbinil. These results indicate that the major form of dihydrodiol dehydrogenase is identical to 17 beta-hydroxysteroid dehydrogenase and the minor enzyme form to aldehyde reductase.
从雄性ddY小鼠的肝脏胞液中分别与17β-羟基类固醇脱氢酶和醛还原酶共纯化得到了主要和次要形式的二氢二醇脱氢酶，纯度达到表观均一。两种酶形式的二氢二醇脱氢酶以及睾酮脱氢酶或醛还原酶的活性在电泳中迁移一致。该酶的主要形式氧化17β-羟基类固醇和非甾体脂环醇，并还原17-酮类固醇和各种合成羰基化合物，对类固醇的亲和力高于对外源生物活性物质的亲和力。这种酶形式对苯二氢二醇和睾酮的活性表现出相同的热稳定性以及对槲皮苷、巯基试剂、非甾体雌激素和抗炎剂抑制作用的敏感性。另一方面，该酶的次要形式氧化苯二氢二醇但不氧化17β-羟基类固醇，也能很好地还原各种醛类，并且被巴比妥类药物和索比尼尔特异性抑制。这些结果表明，二氢二醇脱氢酶的主要形式与17β-羟基类固醇脱氢酶相同，次要酶形式与醛还原酶相同。
