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Studies on the Biosynthesis of 5-Cholestan-3ß-ol

I. CHOLESTENONE 5-REDUCTASE OF RAT LIVER

From the ¹ From the Department of Laboratory Diagnosis, Public Health Research Institute of the City of New York, Inc., and the Bureau of Laboratories, New York City Department of Health, New York, New York 10009

1. Cholest-4-en-3-one 5-reductase of rat liver, which catalyzes the conversion of cholest-4-en-3-one to 5-cholestan-3-one, was shown to be localized mainly in the microsomal fraction.

2. Cholest-4-en-3-one 5-reductase required reduced nicotinamide adenine dinucleotide phosphate as electron donor and differed from the known ⁴-3-ketosteroid 5-reductases by being inactive in the presence of reduced nicotinamide adenine dinucleotide.

3. The microsomal cholest-4-en-3-one 5-reductase preparations did not reduce the double bond of cholest-4-en-3ß-ol, cholesterol, or cholest-5-en-3-one.

4. The action of cholest-4-en-3-one 5-reductase was inhibited by certain ⁴-3-ketosteroids and by cholest-5-en-3-one, and appeared to be stimulated by cholesta-4,6-dien-3-one and by cholesta-5,7-dien-7-one.

5. It was concluded that the microsomal cholest-4-en-3-one 5-reductase of rat liver is not identical with the known microsomal ⁴-3-ketosteroid 5-reductases.

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