Abstract
Extensive studies on carbonyl reducing enzymes in recent years have led to the establishment of the aldo-keto reductase family, members of which are aldehyde reductase (EC 1.1.1.2) and aldose reductase (EC 1.1.1.21) (Bohren et al, 1989). In addition to these “classic” aldo-keto reductases, enzymes like carbonyl reductase (EC 1.1.1.184), dihydrodiol dehydrogenase (EC 1.3.1.20), NAD(P)H:quinone-oxidoreductase (EC 1.6.99.2) and several hydroxysteroid dehydrogenases (3α-, 17ß-, 20α-, 3α/20ß-) were also shown to be involved in the reductive metabolism of xenobiotic carbonyl compounds (for Review see Maser, 1994). The involvement of hydroxysteroid dehydrogenases in the reductive metabolism of xenobiotic carbonyl compounds and in the inactivation of proximal carcinogens, derived from polycyclic aromatic hydrocarbons, points to other important roles of these proteins besides their normal endocrinological function.
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Maser, E., Oppermann, U.C.T. (1995). Molecular Cloning and Sequencing of Mouse Hepatic 11ß-Hydroxysteroid Dehydrogenase/Carbonyl Reductase. In: Weiner, H., Holmes, R.S., Wermuth, B. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 5. Advances in Experimental Medicine and Biology, vol 372. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1965-2_27
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DOI: https://doi.org/10.1007/978-1-4615-1965-2_27
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