Abstract
Abstract Pursuant to the observation that milk xanthine oxidase utilizes the carbonyl but not the gem diol form of acetaldehyde, other aldehyde-utilizing enzymes have been similarly investigated. The aldehyde dehydrogenase of yeast and the xanthine dehydrogenase of chicken liver have also been shown to act upon the carbonyl rather than the hydrated form of aldehydes. The similar preference of yeast alcohol dehydrogenase has been confirmed. The reported ability of glyceraldehyde 3-phosphate dehydrogenase to act upon acetaldehyde and butyraldehyde is questioned on the basis of observations that these freshly distilled aldehydes are not substrates but become active as substrates when incubated in aqueous solutions. Aldol is active as a substrate of this enzyme, and the data suggest that aldol condensation products of acetaldehyde and of butyraldehyde are the substrates generated in aqueous solutions of these aldehydes.
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