Abstract

Purified alcohol dehydrogenase from Drosophila melanogaster is able to catalyze the oxidation of aldehydes in addition to primary and secondary alcohols. Acetaldehyde, methoxy-acetaldehyde, chloro-acetaldehyde, and trichloro-acetaldehyde (chloral hydrate) are used here to show that the gem-diol structure is the reacting form of the aldehydes. The reaction rates depend primarily on the degree of hydration of the aldehydes and to a lesser extent on the resulting electronic state of the hydrated molecules. These results resemble the chemical oxidation of aldehydes. The V K m values for the oxidation of acetaldehyde hydrate and chloro-acetaldehyde hydrate are very similar to that for ethanol. The very high oxidation rates of secondary alcohols compared to primary alcohols by Drosophila ADH are explained as the result of the structural resemblance to hydrated aldehydes and a more favorable electronic state. This behavior is in contrast to mammalian and yeast ADH, which have a low affinity for secondary alcohols and aldehydes. The oxidation of aldehydes by ADH apparently enables D. melanogaster to live in alcoholic environments.

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