The oxidation of 2,5-dihydroxypyridine has been studied with a highly purified oxygenase obtained in crystalline form. The reaction consumes 1 mole of oxygen and yields 1 mole of formate per mole of substrate. Maleamate is a second product of the reaction. N-Formylmaleamic acid could not be detected as an intermediate of the reaction and synthetic N-formylmaleamate was not a substrate for the enzyme. The distribution of oxygen 18 from 18O2 and H218O in the products confirmed the dioxygenase nature of the enzyme. The data indicate that addition of molecular oxygen and hydrolytic cleavage of the N-formyl group are catalyzed by a single enzyme.
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Gauthier et al. (1971) studied this question.
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