L-lysine 6-oxidase

In enzymology, a L-lysine 6-oxidase (EC 1.4.3.20) is an enzyme that catalyzes the chemical reaction

L-lysine + O₂ + H₂O 2-aminoadipate 6-semialdehyde + H₂O₂ + NH₃

The 3 substrates of this enzyme are L-lysine, O₂, and H₂O, whereas its 3 products are 2-aminoadipate 6-semialdehyde, H₂O₂, and NH₃.

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

IUBMB entry for 1.4.3.20
BRENDA references for 1.4.3.20 (Recommended.)
PubMed references for 1.4.3.20
PubMed Central references for 1.4.3.20
Google Scholar references for 1.4.3.20
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: 2493–501. doi:10.1128/JB.188.7.2493-2501.2006. 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: 1577–85. PMID 17030025.