The oxidative demethylation of the model substrate ethylmorphine has been characterized for the first time in the liver of a fish (Poecilia reticulata). The enzyme showed maximal activity at 35 degrees C and pH values higher than 8. The values of Km and Vmax for the reaction were 0.83 +/- 0.11 mM and 4.64 +/- 0.81 nmol HCHO/(mg microsomal protein) per min. The activity is attributed to the cytochrome P-450-dependent monoxygenase system, since it is inhibited by CO and requires NADPH; moreover it is inhibited competitively by alpha-naphthoflavone and non-competitively by metyrapone. The enzyme activity is induced by a two-week treatment of fish with phenobarbital and may be associated with a protein band of Mr 54,000.
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