Abstract
Mammalian hydroxysteroid dehydrogenases (HSDs) regulate the occupancy of steroid hormone receptors by interconverting active hormones with their cognate inactive metabolites. In this manner, they work as molecular switches that control steroid hormone action. Specificity is achieved by reducing carbonyl groups to hydroxyl groups in a positional and stereoselective manner on the steroid nucleus or steroid side-chain. cDNA cloning indicates that HSDs belong to two distinct protein phylogenies: the aldo-keto reductase (AKR) superfamily (Pawlowski et al., 1991; Lacy et al., 1993; Warren et al., 1993; Mao et al., 1994) and the short-chain dehydrogenase/reductase family (SDR, formerly known as the short-chain alcohol dehydrogenase family) (Krozowski, 1994; Jörnvall et al., 1995).
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Penning, T.M. (1996). Hydroxysteroid Dehydrogenases. In: Weiner, H., Lindahl, R., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 6. Advances in Experimental Medicine and Biology, vol 414. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5871-2_54
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DOI: https://doi.org/10.1007/978-1-4615-5871-2_54
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