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- W2076659478 abstract "Abstract The 3-hydroxysteroid dehydrogenase activity of cortisone reductase (20-dihydrocortisone:NAD+ oxidoreductase, EC 1.1.1.53) was known to be 3α activity in the case of certain 5α-steroids in which 3α was 3R and axial. It is now shown to be 3α activity also in a 5α-steroid in which 3α is 3S and axial. In the 5β series, both 3α, 3R, equatorial activity and 3β, 3S axial activity are now described, though the compounds were very poor substrates. The view is discussed that interactions between the all-trans-5α-steroids and the enzyme distinguish the α side of the steroid from the β side; and that the angled A/Bcis-steroids of the 5β series are either bound somewhat differently, or are possibly bound in more than one way. The 20-hydroxysteroid dehydrogenase activity of cortisone reductase was known to be 20β activity in various cases where 20β was 20R. It is now shown to be 20β activity also in a case where 20β is 20S. In the case of 20 activity, the orientation around C-20 at the moment of hydrogen transfer is evidently fixed relative to both the steroid nucleus and the hydrogen donor or acceptor (presumably enzyme-bound NADH or NAD+) even though rotation about the C-17/C-20 bond is possible." @default.
- W2076659478 created "2016-06-24" @default.
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- W2076659478 date "1972-04-01" @default.
- W2076659478 modified "2023-09-26" @default.
- W2076659478 title "Steric, chiral and conformational aspects of the 3-hydroxy- and 20-hydroxysteroid dehydrogenase activities of cortisone reductase preparations" @default.
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- W2076659478 doi "https://doi.org/10.1016/0005-2744(72)90191-x" @default.
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