The effect of bile acids on liver alcohol dehydrogenase in different mammalian species.
1. The effect of bile acids on the activity of liver alcohol dehydrogenase (L-ADH, EC 1.1.1.1) from different mammalian organisms is species dependent. 2. The kinetic behaviour of purified L-ADH from rat and rabbit liver in presence of deoxycholic acid and with ethanol as substrate shows two rather different patterns: for rabbit enzyme deoxycholic acid acts as a full competitive inhibitor, while for rat enzyme an activation effect is observed, with an increase of both Km and Vmax. Similar patterns are obtained with the steroid substrate 3 beta-hydroxy-5 beta-androstane-17one. 3. These results show that in some species, including man, L-ADH activity can be regulated by bile acids, that could control both ethanol oxidation and their own biosynthesis since L-ADH is involved in both metabolic pathways in liver cell.
D000293:Adolescent; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D001647:Bile Acids and Salts / Q000494:pharmacology*; D002417:Cattle; D002648:Child; D006224:Cricetinae; D003840:Deoxycholic Acid / Q000494:pharmacology; D005260:Female; D006736:Horses; D006801:Humans; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D008322:Mammals / Q000378:metabolism*; D051379:Mice; D008810:Mice, Inbred C57BL; D011817:Rabbits; D051381:Rats; D011919:Rats, Inbred Strains; D013045:Species Specificity
D001647:Bile Acids and Salts; D003840:Deoxycholic Acid; D000429:Alcohol Oxidoreductases