A Possible Functional Relationship between Microsomal Aromatic Aldehyde-Ketone Reductase and Hexose-6-phosphate Dehydrogenase

Abstract
Aromatic ketone reductase activity of microsomes showed a unique cofactor requirement: Addition of NADP and glucose-6-phosphate was as effective as that of an artificial NADPH generating system, whereas NADPH alone served as a cofactor less efficiently. Microsomal aromatic ketone reductase, purified partially from guinea pig liver microsomes after solubilization with Triton X-100, reduced 5β-dihydrotestosterone, aromatic aldehydes, and ketones with NADPH as a cofactor. However, addition of hexose-6-phosphate dehydrogenase, purified from the same source, as an NADPH generator produced about 2 times higher activity than that of yeast glucose-6-phosphate dehydrogenase or NADPH alone.

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