Transformation of 3-hydroxy-steroids by Fusarium moniliforme 7alpha-hydroxylase.
Transformation of physiologically important 3-hydroxy-steroids by the DHEA-induced 7alpha-hydroxylase of F. moniliforme was investigated. Whereas DHEA was almost totally 7alpha-hydroxylated, PREG, EPIA and ESTR were only partially converted into their 7alpha-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 7alpha-hydroxylation for these substrates were determined and confirmed that DHEA was the best substrate of the 7alpha-hydroxylase. Inhibition studies of DHEA 7alpha-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 7alpha-hydroxylase of F. moniliforme.
Cotillon
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AC
Laboratoire de Biotechnologie, Conservatoire National des Arts et Métiers, Paris, France.
Morfin
R
R
D000738:Androsterone / Q000378:metabolism; D001189:Aryl Hydrocarbon Hydroxylases; D001665:Binding Sites; D003577:Cytochrome P-450 Enzyme System / Q000096:biosynthesis*; D003687:Dehydroepiandrosterone / Q000378:metabolism; D004790:Enzyme Induction; D004970:Estrone / Q000378:metabolism; D005670:Fusarium / Q000378:metabolism*; D006914:Hydroxysteroids / Q000378:metabolism*; D008861:Microsomes / Q000378:metabolism; D011284:Pregnenolone / Q000378:metabolism; D013250:Steroid Hydroxylases / Q000096:biosynthesis*
D006914:Hydroxysteroids; D004970:Estrone; D003687:Dehydroepiandrosterone; D011284:Pregnenolone; D003577:Cytochrome P-450 Enzyme System; D000738:Androsterone; D013250:Steroid Hydroxylases; D001189:Aryl Hydrocarbon Hydroxylases; C029009:steroid hormone 7-alpha-hydroxylase