L-lysine 6-oxidase
| L-lysine 6-oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.3.20 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, L-lysine 6-oxidase (EC 1.4.3.20) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are L-lysine, water, and oxygen. Its products are L-allysine, hydrogen peroxide, and ammonia.[1][2][3]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-lysine:oxygen 6-oxidoreductase (deaminating). Other names in common use include L-lysine-epsilon-oxidase, Lod, LodA, and marinocine.
References
- ^ Enzyme 1.4.3.20 at KEGG Pathway Database.
- ^ Lucas-Elio P, Gomez D, Solano F, Sanchez-Amat A (2006). "The antimicrobial activity of marinocine, synthesized by Marinomonas mediterranea, is due to hydrogen peroxide generated by its lysine oxidase activity". J. Bacteriol. 188 (7): 2493–501. doi:10.1128/JB.188.7.2493-2501.2006. PMC 1428416. PMID 16547036.
- ^ Gomez D, Lucas-Elio P, Sanchez-Amat A, Solano F (2006). "A novel type of lysine oxidase: L-lysine-epsilon-oxidase". Biochim. Biophys. Acta. 1764 (10): 1577–85. doi:10.1016/j.bbapap.2006.08.014. PMID 17030025.