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- W1845202224 abstract "This study was conducted to evaluate further the reaction catalyzed by the saturated steroid 6α-hydroxylase of extrahepatic human tissues. Progesterone and 5α-dihydroprogesterone (5α-DHP) are plasma-borne precursors of 5α-pregnan-3α-ol-20-one, an anxiolytic/anesthetic steroid, and 5α-pregnan-3β-ol-20-one in extrahepatic human tissues. These two steroids are metabolized further by a saturated steroid 6α-hydroxylase enzyme(s) that is distinct from the cytochrome P450 6α-hydroxylase that catalyzes the 6α-hydroxylation ofΔ 4-3-ketosteroids such as progesterone, cortisol, and testosterone. Products of this saturated steroid 6α-hydroxylase, viz. 3β/α,6α-dihydroxy-5α-pregnan-20-ones, are major radiolabeled urinary metabolites (excreted as glucuronosides) of iv administered tritium-labeled 5α-DHP in women and men. T47-D human breast cancer cells, which are rich in saturated steroid 6α-hydroxylase activity, were used as the enzyme source in this study. The greatest total and the highest specific activity of saturated steroid 6α-hydroxylase were localized in microsome-enriched preparations; enzyme activity was linear with incubation time up to 30 min and with microsome-enriched tissue protein concentrations between 0.05–0.5 mg/mL incubation mixture. The velocity of the reaction was similar in incubations in which the pH was varied from 6.0–8.0, and NADH and NADPH were equally effective in supporting the 6α-hydroxylation of 5α-pregnan-3β-ol-20-one and 5α-pregnan-3α-ol-20-one. The more efficient substrates for this enzyme were 5α-pregnan-3β-ol-20-one and 5α-pregnan-3α-ol-20-one, and the apparent Km (∼3.5 μmol/L) and maximum velocity (∼150 pmol/min·mg microsome-enriched protein) for these two substrates were indistinguishable. 5α-Androstane-3β,17β-diol was less efficiently 6α-hydroxylated, and 5α-androstane-3α,17β-diol was an inefficient substrate. The addition of a variety of inhibitors of cytochrome P450 monooxygenases to the incubation mixtures did not diminish significantly the 6α-hydroxylation of 5α-pregnan-3β-ol-20-one, findings consistent with those of other investigators who suggested that human saturated steroid 6α-hydroxylase (of human prostate) is not a cytochrome P450." @default.
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- W1845202224 date "1997-05-01" @default.
- W1845202224 modified "2023-10-16" @default.
- W1845202224 title "Human Saturated Steroid 6α-Hydroxylase1" @default.
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- W1845202224 doi "https://doi.org/10.1210/jcem.82.5.3908" @default.
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