Abstract
Four mammalian class I liver alcohol dehydrogenases catalyze stereospecific oxidoreduction at the 3-position of 5β-steroids: the horse S, human γ, rat and rabbit enzymes (Waller et al., 1965; McEvily et al., 1988; Reynier et al., 1975; Höög et al., 1993). These enzymes may provide a connection between the metabolism of ethanol and steroids, since alcohol oxidation raises the NADH/NAD+ ratio in the liver and thus shifts the redox state in favor of the reduced steroid (Anderson et al., 1986). Evaluating the role of liver alcohol dehydrogenase in steroid metabolism requires more complete knowledge of substrate specificities, kinetic parameters and species variation.
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Strasser, F., Huyng, M.N., Plapp, B.V. (1996). Activity of Liver Alcohol Dehydrogenases on Steroids. 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_36
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DOI: https://doi.org/10.1007/978-1-4615-5871-2_36
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