The partial purification of the enzyme, aromatic aldehyde-ketone reductase (aromatic A-K reductase), from rabbit kidney cortex is described. Aromatic A-K reductase utilizes TPNH but not DPNH as a cosubstrate. Substituted benzaldehydes and acetophenones are readily reduced to carbinols. Aromatic A-K reductase does not, however, catalyze the reverse reaction, the dehydrogenation of carbinols under the experimental conditions used. Aromatic A-K reductase utilizes the β hydrogen atom at C-4 of TPNH.
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Culp et al. (1968) studied this question.
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