Properties of hydroxysteroid oxidoreductase isolated from yeast

Yeasts can advantageously be utilized for the production of the 17beta-hydroxy-derivative, from 3-methoxy-8,14-seco-1,3,5(10),9(11)-estratetraene-14,17-dione (14,17-dione) while 14alpha-hydroxy and 14alpha,17beta-dihydroxy-derivatives are also formed. The biochemical properties of yeasts' enzymes responsible for the formation of the two monohydroxy-derivatives have been studied in detail. In the cell-free extract of Saccharomyces the presence of two hydroxysteroid oxidoreductases could be detected. The first enzyme forms 3beta,17beta-dihydroxy-derivative from 5alpha-androstane-317-dione. This enzyme is responsible for the formation of 17beta-hydroxy-derivative from 14,17-dione. The second enzyme forms 3alpha-hydroxy-derivative from 5beta-androstanedione as well as 14alpha-hydroxy-derivative from its 14,17-dione. The cofactor of both enzymes is pyridine nucleotide. The two enzymes possessing different properties can selectively be inhibited.