Abstract
1. 1. The oxidation of racemic 2-hydroxyputrescine ( d,l-1,4-diamino-2-hydroxy-butane) and 2-hydroxycadaverine ( d,l-1,5-diamino-2-hydroxypentane) was investigated by using partially purified pea-seedling and pig-kidney diamine oxidase (diamine: oxygen oxidoreductase (deaminating), EC 1.4.3.6). The effects of pH, enzyme and substrate concentration were studied. 2. 2. The activities of both enzymes towards hydroxydiamines were lower than those towards putrescine or cadaverine at the pH optimum for each substrate. The oxidation entailed the consumption of 1 atom of oxygen, in the presence of catalase, with the formation of 1 mole of ammonia and 1 mole of the corresponding cyclic ω-aminoaldehyde, i.e. the hydroxy derivatives of Δ 1-pyrroline and Δ 1-piperideine, respectively. 3. 3. Evidence for the spontaneous conversion of the oxidation product of hydroxyputrescine to pyrrole is presented.
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