Relative reactivities of primary alcohols as substrates of liver alcohol dehydrogenase

Abstract

To obtain information concerning the general structural requirement of alcohols as substrates of liver alcohol dehydrogenase, the kinetics of the enzymic oxidation of primary alcohols were studied. All the active substrates possess hydrophobic side groups. Introduction of polar groups renders alcohols inactive or inhibitory. To correlate reactivities of primary alcohols as substrates with the nature of their side groups, their relative reactivities are expressed in terms of kinetic coefficients which were solved from the rate equation by successive graphical analysis. Based on kinetic results, the relative reactivities of primary alcohols as substrates of liver alcohol dehydrogenase are discussed in relation to the hydrophobic interaction and the electronic effect of their side groups.