Abstract
Enzyme(s) catalyzing the conversion of androst-5-ene-3,17-dione (I) to the corresponding Δ 4 -3-ketone have been found in a number of rat tissues with the highest specific activity residing in the adrenal. Bovine adrenal homogenates demonstrated Δ 5 -3-keto isomerase activity in the soluble, mitochondrial and microsomal fractions with the greatest enzyme concentration in the particulate fractions. Acetone powders prepared from the three bovine adrenal fractions effected the isomerization of I, of pregn-5-ene-3,20-dione (II) and of 17α-methyl-17β-hydroxyandrost-5-en-3-one (III) while cholest-5-en-3-one was not affected, in each fraction the isomerization of I and of II was shown to be catalyzed by separate enzymes although I and III were substrates for the same enzyme. Progesterone markedly inhibited the isomerization of II and to a lesser extent, the isomerization of I. There appears to be no coenzyme requirement for isomerase activity.
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