PuSH - Publication Server of Helmholtz Zentrum München: Human liver debrisoquine 4-hydroxylase: Test for specifity toward various monooxygenase substrates and model of the active site.

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Wolff, T. ; Distlerath, L.M.* ; Worthington, M.T.* ; Guengerich, F.P.*

Human liver debrisoquine 4-hydroxylase: Test for specifity toward various monooxygenase substrates and model of the active site.

Arch. Toxicol. 60, 89-90 (1987)

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Polyclonal antibodies raised toward a debrisoquine 4-hydroxylating cytochrome P-450 species purified from rat liver (P-450UTA) were used to determine which monooxygenase reactions are linked to debrisoquine hydroxylation in human liver. Anti P-450UTA did not inhibit the oxidation of dimethylnitrosamine, morphine, diazepam, vinylidene chloride, trichloroethylene, benzo(a)pyrene and its 7.8-dihydrodiol, but was inhibitory for the hydroxylation of debrisoquine, (±)-bufuralol, lasiocarpine and monocrotaline. A model interpreting the substrate specificity of the human liver enzyme is presented. .

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