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The Cu(2+)-Zn(2+) superoxide dismutase of human erythrocytes (HED) catalyzes the oxidation of alkyl amines. The optimal pH for the catalytic activity was 8.8 and the enzyme showed a similar catalytic efficiency for the oxidation of ethyl and propyl amines. Ethyl and propyl amines were also oxidized in the presence of their substrates with enhancement of the rates of substrate oxidation. The reaction rates were linearly dependent on substrate concentrations, thus indicating the monomolecular character of the enzyme-substrate complex and the random mechanism of the reaction. The catalytic efficiency decreased in the order of propyl > ethyl > butyl > benzyl. Monodansylcadaverine covalently attached to the HED inactive site was oxidized by alkylamines. The stoichi
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