Steroid oxidoreductase activity of alcohol dehydrogenases from horse, rat, and human liver.
Alcohol dehydrogenase from horse (isoenzyme SS and ES, but not EE), rat and human liver were found to catalyze the NAD-dependent oxidation of 3beta-hydroxy groups in 5alpha- and 5beta-steroids of the C19, C21, and C24 series. The enzymes from horse and rat liver were more active on 5beta-than on 5alpha-steroids. This difference was most marked with the enzyme from rat liver, especially with 3beta-hydroxyandrostan-17-ones and 3beta-hydroxypregnan-20-ones as substrates. The Km of isoenzyme ES from horse liver was lower for 3beta-hydroxy-5alpha-cholanoic acid (0.4 muM) than for 3beta-hydroxy-5beta-cholanoic acid (0.9 muM). 3alpha-Hydroxysteroids were not substrates for the enzymes from horse and rat liver. Human liver alcohol dehydrogenase had low affinity for 3beta-hydroxy-5alpha (and 5beta)-cholanoic acids, but oxidation could be clearly demonstrated by gas chromatographic analysis of the products.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D006736:Horses; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D010088:Oxidoreductases / Q000378:metabolism*; D051381:Rats; D013045:Species Specificity
D007527:Isoenzymes; D009243:NAD; D010088:Oxidoreductases; D000429:Alcohol Oxidoreductases