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• W2016995822 abstract "Abstract Lysine monooxygenase, a pseudomonad flavoprotein, was almost inactive with an α-monoamino acid as substrate, but the addition of an alkylamine, a counterpart of the fragmented lysine molecule, caused marked oxygen consumption. The rate of oxygen consumption was examined and compared with various combinations of α-monoamino acids and alkylamines. Hydrogen peroxide was formed and the corresponding α-keto acid was produced from each amino acid. In most cases, the hydrogen peroxide formation was nearly equal to the oxygen consumption. In some other cases, however, the oxygen consumption exceeded the hydrogen peroxide formation, and the production of an acid amide in addition to the α-keto acid was qualitatively demonstrated. Thus, both an oxidative deamination and an oxygenative decarboxylation of the same substrate occurred concomitantly, although the ratio of the two types of reaction varied with different combinations of amino acids and alkylamines. Alkylamines at higher concentrations competitively inhibited the lysine oxygenation, whereas lower concentrations of alkylamines stimulated the lysine oxygenation by decreasing the sigmoidicity of the saturation curve for lysine. These results suggest a dual function of the alkylamine; i.e., the interaction with the active site as a fragment of substrate and the effect on the regulatory property of the enzyme." @default.
• W2016995822 created "2016-06-24" @default.
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• W2016995822 date "1975-11-01" @default.
• W2016995822 modified "2023-09-25" @default.
• W2016995822 title "Alkylamine-dependent oxidation and oxygenation of α-monoamino acids by lysine monooxygenase" @default.
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• W2016995822 doi "https://doi.org/10.1016/0003-9861(75)90038-7" @default.
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