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- W1653072259 abstract "The conversion of 4-cholesten-3-one into 5β-cholestan-3-one (coprostanone) by microorganisms in caecal contents from rats has been studied. The enzyme activity was present in the soluble part of a homogenate obtained by freeze-pressing of caecal contents of rats. The major part of the activity could be precipitated between 25 and 50% saturation with ammonium sulphate. The 3-oxo-Δ4-steroid 5β-reductase activity required NADH as cofactor and was inhibited by p-chloromercuribenzoate. The enzyme preparation also catalyzed the reduction of the Δ4-double bond in progesterone and testosterone but did not catalyze reduction of the Δ5-double bond in cholesterol, pregnenolone or dehydroepiandrosterone. The rate of reduction of the Δ4-double bond in progesterone was more than twice as fast as the rate of reduction of the Δ4-double bond in 4-cholesten-3-one. The mechanism of reduction of Δ4-double bonds in 3-oxo-Δ4-steroids by the microbial 3-oxo-Δ4-steroid 5β-reductase was found to involve transfer of hydrogen from the 4B-position of NADH to the 5β-position of the steroid." @default.
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- W1653072259 date "1973-08-01" @default.
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- W1653072259 title "Microbial Transformation of Cholesterol into Coprostanol. Properties of a 3-Oxo-Delta4-Steroid-5beta-Reductase" @default.
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- W1653072259 doi "https://doi.org/10.1111/j.1432-1033.1973.tb02968.x" @default.
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