Separation and properties of multiple forms of dihydrodiol dehydrogenase from hamster liver.

1. Five multiple forms of dihydrodiol dehydrogenase (EC 1.3.1.20) with similar molecular weights of around 35,000 were purified from hamster liver cytosol. 2. All the enzymes oxidized trans-dihydrodiols of benzene and naphthalene and reduced various carbonyl compounds, but showed clear differences in specificities for other alcohols and cofactors, and in inhibitor sensitivity. 3. Two NADP+-dependent enzymes were immunologically identified with aldehyde reductase (EC 1.1.1.2) and 3 alpha-hydroxytsteroid dehydrogenase (EC 1.1.1.50). 4. The other enzymes with dual cofactor specificity oxidized xenobiotic alicyclic alcohols, and one of them was active on 3 alpha- and 17 beta-hydroxysteroids with NAD+ as a preferable cofactor.