In enzymology, L-lysine oxidase (EC 1.4.3.14) is an enzyme that catalyzes the chemical reaction
| L-lysine oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.3.14 | ||||||||
| CAS no. | 70132-14-8 | ||||||||
| 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 | ||||||||
| |||||||||
The three substrates of this enzyme are L-lysine, water, and oxygen. Its products are 6-amino-2-oxohexanoic acid, 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 2-oxidoreductase (deaminating). Other names in common use include L-lysine alpha-oxidase, and L-lysyl-alpha-oxidase. This enzyme participates in lysine degradation.[1]
References
edit- 1 2 Enzyme 1.4.3.14 at KEGG Pathway Database.
- ↑ 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. doi:10.1016/S0021-9258(19)86128-8. PMID 6101334.
- ↑ Lukasheva, EV; Berezov, TT (October 2002). "L-Lysine alpha-oxidase: physicochemical and biological properties". Biochemistry (Moscow). 67 (10): 1152–8. doi:10.1023/A:1020967408229. PMID 12460113.
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