Kinetic Studies on the Amine Oxidase Reaction

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The reaction of amine oxidase [monoamine: oxygen oxidoreductase (deaminating), EC 1. 4. 3. 4] from Aspergillus niger was analyzed from data on the overall reaction rate and from data obtained by the “stopped” and “continuous flow” methods. π-Butylamine, benzylamine, and ethylamine were mainly used as substrates. The steady state spectra of the enzyme (steady state minus PMP level) obtained with various substrates under aerobic conditions were different; absorption maxima were observed at 335, 420, and 495 mμ with π-butylamine, at 375 and 495 mμ with benzylamine, at 420 and 495 mμ with ethylamine, and at 335, 400, and 495 mμ with histamine. The following scheme was proposed as the mechanism of the amine oxidase reaction to account for these data. where El and EM are the PLP and PMP forms of the enzyme unit, respectively, X and Y are intermediates and P is the product.