Abstract
The kinetics of the enzyme reaction of ethanol and propanol oxidation and acetaldehyde and propionaldehyde reduction catalyzed by alcohol dehydrogenase (ADH) (EC 1.1.1.1) isolated from germinating broad bean seeds proceed according to the bi-bi ordered mechanism of Theorell and Chance. The p H optimum for the oxidation of ethanol is 8.7 and for the oxidation of propanal 9.2; the p H optimum for the reduction of acetaldehyde is 7.1 and for the reduction of propionaldehyde 7.3. The reaction catalyzed by broad bean ADH was inhibited by adenosine and AMP. It was found that inhibition is competitive with respect to NAD. Inhibition by AMP is p H-dependent and by adenosine p H-independent. From the competitive inhibition it follows that the adenine part of NAD is important for bonding of the coenzyme to ADH. The phosphate groups also influence the enzyme-coenzyme interaction.
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