A Novel Dihydrodiol Dehydrogenase in Bovine Liver Cytosol: Purification and Characterization of Multiple Forms of Dihydrodiol Dehydrogenase

• Published in: Journal of biochemistry (Tokyo) 1992-10, Vol.112 (4), p.523-529
• Main Authors: Mizoguchi, Tadashi, Nanjo, Hirofumi, Umemura, Toshifumi, Nishinaka, Tohru, Iwata, Chuzo, Imanishi, Takeshi, Tanaka, Tetsuaki, Terada, Tomoyuki, Nishihara, Tsutomu
• Format: Article
• Language: English
• Subjects: 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific); 3-Hydroxysteroid Dehydrogenases - antagonists & inhibitors; 3-Hydroxysteroid Dehydrogenases - isolation & purification; 3-Hydroxysteroid Dehydrogenases - metabolism; Alcohol Oxidoreductases - antagonists & inhibitors; Alcohol Oxidoreductases - isolation & purification; Alcohol Oxidoreductases - metabolism; Aldehyde Reductase - antagonists & inhibitors; Aldehyde Reductase - isolation & purification; Aldehyde Reductase - metabolism; Analytical, structural and metabolic biochemistry; Androsterone - pharmacology; Animals; Biological and medical sciences; Cattle; characterization; Cross Reactions; Cytosol - enzymology; dihydrodiol dehydrogenase; Enzymes and enzyme inhibitors; Female; Fundamental and applied biological sciences. Psychology; Isoenzymes - antagonists & inhibitors; Isoenzymes - isolation & purification; Isoenzymes - metabolism; liver; Liver - enzymology; Molecular Weight; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; purification; Rabbits; Sensitivity and Specificity; Subcellular Fractions - enzymology; Substrate Specificity
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/oxfordjournals.jbchem.a123932

Three enzymes (DD1, DD2, and DD3) having dihydrodiol dehydrogenase activity were purified to homogeneity from bovine liver cytosol. DD1 and DD2 were identified as 3α-hydroxysteroid dehydrogenase and high-Km aldehyde reductase, respectively, as judged from their molecular weights, substrate speclflcities and Inhibitor sensitivities. DD3 was a unique enzyme which could specifically catalyze the dehydrogenatlon of trans-benzenedihydrodlol and trans-naphthalenedlhydrodiol without any activity toward the other tested alcohols, aldehydes, ketones, and quinones. The Km value of DD3 (0.18 mM) for benzenedlhydrodiol was lower than those of other dihydrodlol dehy drogenases so far reported. DD3 immunologically crossreacted with DD1, but showed no crossreactivlty with DD2. Additionally, DD3 was inhibited In a competitive manner, with a low K1 value of 1 μM, by androsterone, which was a good substrate for DD1. It was assumed that DD3 isa novel enzyme which is specific to dihydrodiols, exhibiting similarity to DD1 in immunological and structural properties.