Esterase activity of liver alcohol dehydrogenase

Abstract

Liver alcohol dehydrogenase is found to possess, in addition to its dehydrogenase and dismutase activities, the ability to hydrolyze octanoate esters at a rate approximately 1 500 – 1 1000 of that of the dehydrogenase reaction. The esterase and dehydrogenase activities exhibit an identical isozyme pattern indicating that the same protein catalyzes both reactions. Inhibition studies suggest that the esterase activity presumably shares the catalytic domain with the dehydrogenase activity.