Abstract
The enzyme 3β-hydroxysteroid dehydrogenase/Δ5-Δ4 isomerase (3β-HSD) catalyzes the transformation of Δ5-ene, 3β-hydroxy to Δ4-3-keto steroids and is therefore an essential enzyme in the biosynthesis of all steroid hormones. 3β-HSD deficiency results in decreased formation of cortisol, aldosterone, and sex steroids (1). Clinically, 3β-HSD deficiency causes ambiguous genitalia and lethal adrenal insufficiency in newborns (2). On the other hand, the reversible interconversion of Δ5-androstenediol to DHEA, testosterone to Δ4-androstenedione, and estrone to estradiol is mediated by 17β-hydroxysteroid dehydrogenase (17β-HSD), also termed 17-oxidoreductase or 17-ketosteroid reductase. Deficient activity of ovarian 17β-HSD can cause hirsutism and polycystic ovarian disease (3). 3β-HSD and 17β-HSD are both non-cytochrome P-450 enzymes using NAD and NADPH as cofactors, respectively.
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© 1991 Springer-Verlag New York, Inc.
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Tremblay, Y., Marcotte, B., Strauss, J.F. (1991). Differential Regulation of 3β-HSD and 17β-HSD Expression in Granulosa Cells. In: Gibori, G. (eds) Signaling Mechanisms and Gene Expression in the Ovary. Serono Symposia USA. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3200-1_26
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DOI: https://doi.org/10.1007/978-1-4612-3200-1_26
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