Abstract
Microsomes from Nicotiana otophora catalyze the demethylation of nicotine to nornicotine in the presence of NADPH and oxygen. Activity was maximal at pH 7.0-7.5 and 30 o C. The enzyme appeared to be most stable in the presence of both nicotine and NADPH. Phosphate, magnesium, nornicotine, and concentrations of microsomal protein higher than 2 mg/mL were inhibitory. Typical rates of nornicotine formation were 10-50 pmol min -1 (mg of protein) -1 , while V max and the apparent K m (nicotine) were estimated to be 105 pmol/min and 51 μM, respectively (.)
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