L-lizin 6-oksidaza
(Preusmjereno sa stranice Lod)
| L-lizin 6-oksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.4.3.20 | ||||||||
| CAS broj | 1116448-48-6 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
L-lizin 6-oksidaza (EC 1.4.3.20, L-lizin-epsilon-oksidaza, Lod, LodA) je enzim sa sistematskim imenom L-lizin:kiseonik 6-oksidoreduktaza (deaminacija).[1][2] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-lizin + O2 + H2O (S)-2-amino-6-oksoheksanoat +H2O2 + NH3
Ovaj enzim se razlikuje od EC 1.4.3.13, protein-lizin 6-oksidaza, po tome što koristi slobodan L-lizin umesto za protein-vezane forme. N2-acetil-L-lizin je takođe supstrat, dok N6-acetil-L-lizin nije.
- ↑ Lucas-Elío, P., Gómez, D., Solano, F. and 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: 2493-2501. PMID 16547036.
- ↑ Gómez, D., Lucas-Elío, P., Sanchez-Amat, A. and Solano, F. (2006). „A novel type of lysine oxidase: L-lysine-ε-oxidase”. Biochim. Biophys. Acta 1764: 1577-1585. PMID 17030025.
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