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• W1578973863 abstract "The substrate specificity of the microsomal hydroxylating system has been further investigated. The products of the reactions are phenols in all cases studied, as well as a dihydrodiol in the case of naphthalene, and a dihydrodiol-like compound in the case of quinoline. The conversion of indole to 3-hydroxyindole has been demonstrated. This finding raises the possibiltiy that the indican of the urine might be derived from hydroxylation of indole in the liver rather than from hydroxylation by bacteria in the gut. Evidence is presented for the presence of a family of hydroxylating enzymes in liver microsomes. Although it was not possible to solubilize the hydroxylating enzymes, it was possible to obtain enzymically active microsomal fragments. DPNH was considerably less active than TPNH as a cofactor for the hydroxylation of acetanilide by microsomes from nine animal species. On the contrary, where it was possible to show a stimulation of activity by a reduced pyridine nucleotide, DPNH was more effective than TPNH as a cofactor for the soluble phenylalanine hydroxylase." @default.
• W1578973863 created "2016-06-24" @default.
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• W1578973863 date "1961-08-01" @default.
• W1578973863 modified "2023-10-17" @default.
• W1578973863 title "Enzymic hydroxylation of aromatic compounds" @default.
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• W1578973863 doi "https://doi.org/10.1016/0003-9861(61)90041-8" @default.
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