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Arginine 2-monooxygenase (EC 1.13.12.1) is an enzyme that catalyzes the chemical reaction

L-arginine + O₂ ${\displaystyle \rightleftharpoons }$ 4-guanidinobutanamide + CO₂ + H₂O

Thus, the two substrates of this enzyme are L-arginine and oxygen, whereas its 3 products are 4-guanidinobutanamide, carbon dioxide, and water.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O₂ as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O with incorporation of one atom of oxygen (internal monooxygenases o internal mixed-function oxidases). The systematic name of this enzyme class is L-arginine:oxygen 2-oxidoreductase (decarboxylating). Other names in common use include arginine monooxygenase, arginine decarboxylase, arginine oxygenase (decarboxylating), and arginine decarboxy-oxidase. This enzyme participates in urea cycle and metabolism of amino groups. It has one cofactor: the flavin FAD.

References

• Olomucki A, Pho DB, Lebar R, Delcambe L, Thoai NV (1968). "". Biochim. Biophys. Acta. 151 (2): 353–66. doi:10.1016/0005-2744(68)90102-2. PMID 4295160.
• Thoai NV, Olomucki A (1962). "Arginine decarboxy-oxydase. I. Caracteres et nature de l'enzyme". Biochim. Biophys. Acta. 59 (3): 533–544. doi:10.1016/0006-3002(62)90631-5.
• Thoai NV, Olomucki A (1962). "Arginine decarboxy-oxydase. II. Oxydation de la canavanine et de l'homoarginine en beta-guanidopropionamide et en delta-guanidovaleramide". Biochim. Biophys. Acta. 59: 545–552. doi:10.1016/0006-3002(62)90632-7.

• Biology

• EC 1.13.12
• Flavoproteins
• Enzymes of unknown structure