Arginine 2-monooxygenase
| Arginine 2-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.12.1 | ||||||||
| CAS no. | 9027-36-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Arginine 2-monooxygenase (EC 1.13.12.1) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-arginine and oxygen. Its products are tiformin (4-guanidinobutanamide), carbon dioxide, and water.[1][2]
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: flavin adenine dinucleotide.[3][4]
References
- ^ 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. PMID 14479405.
- ^ 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 (3): 545–552. doi:10.1016/0006-3002(62)90632-7.
- ^ Enzyme 1.13.12.1 at KEGG Pathway Database.
- ^ Olomucki A, Pho DB, Lebar R, Delcambe L, Thoai NV (1968). "[Arginine oxygenase (decarboxylating). V. Purification and flavin nature]". Biochim. Biophys. Acta. 151 (2): 353–66. doi:10.1016/0005-2744(68)90102-2. PMID 4295160.