Lysine 2-monooxygenase
| lysine 2-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.12.2 | ||||||||
| CAS no. | 9031-22-5 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a lysine 2-monooxygenase (EC 1.13.12.2) is an enzyme that catalyzes the chemical reaction
- L-lysine + O2 5-aminopentanamide + CO2 + H2O
Thus, the two substrates of this enzyme are L-lysine and O2, whereas its 3 products are 5-aminopentanamide, CO2, and H2O.
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-lysine:oxygen 2-oxidoreductase (decarboxylating). Other names in common use include lysine oxygenase, lysine monooxygenase, and L-lysine-2-monooxygenase. This enzyme participates in lysine degradation. It employs one cofactor, FAD.
References
- Nakazawa T, Hori K, Hayaishi O (1972). "Studies on monooxygenases. V. Manifestation of amino acid oxidase activity by L-lysine monooxygenase". J. Biol. Chem. 247 (11): 3439–44. PMID 4624115.
- Takeda H, Hayaishi O (1966). "Crystalline L-lysine oxygenase". J. Biol. Chem. 241 (11): 2733–6. PMID 5911646.
- Takeda H, Yamamoto S, Kojima Y, Hayaishi O (1969). "Studies on monooxygenases. I. General properties of crystalline L-lysine monooxygenase". J. Biol. Chem. 244 (11): 2935–41. PMID 5772467.