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. 1983 Aug;19(2):1213-7.
doi: 10.1016/0022-4731(83)90419-3.

Active site-directed irreversible inhibition of 3 beta-hydroxysteroid dehydrogenase from human placenta

Active site-directed irreversible inhibition of 3 beta-hydroxysteroid dehydrogenase from human placenta

Y Chikhaoui et al. J Steroid Biochem. 1983 Aug.

Abstract

To obtain a placental microsome preparation able to convert androstenedione and testosterone specifically to estrogens, 3 beta-hydroxysteroid dehydrogenase must be eliminated. After solubilisation by Triton X-100, the remaining 3 beta-hydroxysteroid dehydrogenase activity is inhibited by 11 alpha-bromoacetoxyprogesterone, an alkylating analogue of progesterone, which behaves as an irreversible active site-directed inhibitor. The enzyme is protected against inactivation and alkylation by steroid and coenzyme substrates. The inhibition is specific to 3 beta-hydroxysteroid dehydrogenase and the estrogen synthetase (aromatase) activity contained in the preparation is not affected by this inhibitor.

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