Separation and properties of multiple forms of dihydrodiol dehydrogenase from hamster liver.Int J Biochem. 1989; 21(4):367-75.IJ
1. Five multiple forms of dihydrodiol dehydrogenase (EC 126.96.36.199) 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 188.8.131.52) and 3 alpha-hydroxytsteroid dehydrogenase (EC 184.108.40.206). 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.