title: Characterization of rat testicular alcohol dehydrogenase.
abstract: A protein from rat testes that catalyzes the oxidation of ethanol in the presence of NAD+, but not NADP+, has been characterized enzymatically and compared to that of hepatic alcohol dehydrogenase obtained from the same animals. The testicular enzyme, like the hepatic enzyme, has a Km value for ethanol in the 0.5-1.0-mM range and can utilize other alcohols such as n-propanol, n-butanol, and isobutanol, although the Km values for these other alcohols are considerably lower (0.03-0.08 mM) that that for ethanol. The testicular enzyme is more heat-labile than is the hepatic enzyme. Finally, the testicular enzyme catalyzes the oxidation of retinol and its retinol dehydrogenase activity is inhibited by ethanol.
mesh_terms: D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002451:Cell Compartmentation; D000077604:Fomepizole; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008297:Male; D011720:Pyrazoles / Q000494:pharmacology; D051381:Rats; D013379:Substrate Specificity; D013737:Testis / Q000201:enzymology*; D014801:Vitamin A / Q000378:metabolism
chemical_list: D011720:Pyrazoles; D014801:Vitamin A; D000077604:Fomepizole; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase