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In enzymology, a L-lysine oxidase (EC 1.4.3.14) is an enzyme that catalyzes the chemical reaction

L-lysine + O₂ + H₂O ${\displaystyle \rightleftharpoons }$ 6-amino-2-oxohexanoate + NH₃ + H₂O₂

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

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 2-oxidoreductase (deaminating). Other names in common use include L-lysine alpha-oxidase, and L-lysyl-alpha-oxidase. This enzyme participates in lysine degradation.

References

• Kusakabe H, Kodama K, Kuninaka A, Yoshino H, Misono H, Soda K (1980). "A new antitumor enzyme, L-lysine alpha-oxidase from Trichoderma viride. Purification and enzymological properties". J. Biol. Chem. 255 (3): 976–81. PMID 6101334.
• Lukasheva, EV; Berezov, TT (October 2002). "L-Lysine alpha-oxidase: physicochemical and biological properties". Biochemistry (Moscow). 67 (10): 1152–8. PMID 12460113.

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