Human liver alcohol dehydrogenase

Human liver alcohol dehydrogenase (Thble 5.3) catalyzes the oxidation of digitalis derivatives. This is a potentially important detoxication pathway. Liver alcohol dehydrogenase may also toxify chemicals. 

Von Wartburg JP, Bethune JL, Vallee BL. Human liver alcohol dehydrogenase. Kinetic and physicochemical properties. Biochemistry 1964 3 1775-1782. 

Kassam JP, Tang BK, Kadar D, Kalow W. In vitro studies of human liver alcohol dehydrogenase variants using a variety of substrates. Drug Metab Dispos 1989 17 567-572. 

Burnell JC, Bosron WF. Genetic polymorphism of human liver alcohol dehydrogenase and kinetic properties of the isoenzymes. In Crow KE, Batt RD, eds. Human Metabolism of Alcohol. Vol. 2. Boca Raton, Florida CRC Press, Inc., 1989 65-75. 

Human liver alcohol dehydrogenase was purified by von Wartburg et al. (59) and crystallized by Mourad and Woronick (60). Chromatograph-ically (61) and electrophoretically (62,63) distinct forms were demon-... 

Yeast and mammalian alcohol dehydrogenases differ in substrate specificity and catalytic activity. The yeast enzyme is more specific for acetaldehyde and ethanol, but mammalian enzymes have a broad substrate specificity, and even with primary alcohols maximum activity is not observed with ethanol. Because of the large amount of alcohol dehydrogenase present in human liver and its role in alcohol metabolism in man, human liver alcohol dehydrogenase is of particular interest. It was first purified by Wartburg et and crystallized by Mourad and Woronick. Human liver alcohol dehydrogenase is a dimer with subunit structures analogous to those of horse liver, and each subunit probably contains two zinc atoms. Several different types of human ADH have been isolated. with minor variations in amino acid... 

Lange LH, Sytkowski J, Vallee BL (1976) Human liver alcohol dehydrogenase purification, composition, and catalytic features. Biochemistry 15 4687-4693... 

---