Abstract
Transformation of physiologically important 3-hydroxy-steroids by the DHEA-induced 7 α-hydroxylase of F. moniliforme was investigated. Whereas DHEA was almost totally 7 α-hydroxylated, PREG, EPIA and ESTR were only partially converted into their 7 α-hydroxylated derivatives because hydroxylation at other undetermined positions as well as reduction of ketone at C17 or C20 into hydroxyl also occurred. Cholesterol was not transformed by the enzyme. Kinetic parameters of the 7 α-hydroxylation for these substrates were determined and confirmed that DHEA was the best substrate of the 7 α-hydroxylase. Inhibition studies of DHEA 7 α-hydroxylation by the other 3-hydroxy-steroids were also carried out and proved that DHEA, PREG, EPIA and ESTR shared the same active site of the enzyme. Induction effects of these steroids were compared, and DHEA appeared to be the best inducer of the 7 α-hydroxylase of F. moniliforme.
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