| EC |
1.4.3.20 |
| Accepted name: |
L-lysine 6-oxidase |
| Reaction: |
L-lysine + O2 + H2O = (S)-2-amino-6-oxohexanoate + H2O2 + NH3 |
| Glossary: |
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
| Other name(s): |
L-lysine-ε-oxidase; Lod; LodA; marinocine |
| Systematic name: |
L-lysine:oxygen 6-oxidoreductase (deaminating) |
| Comments: |
Differs from EC 1.4.3.13, protein-lysine 6-oxidase, by using free L-lysine rather than the protein-bound form. N2-Acetyl-L-lysine is also a substrate, but N6-acetyl-L-lysine, which has an acetyl group at position 6, is not a substrate. Also acts on L-ornithine, D-lysine and 4-hydroxy-L-lysine, but more slowly. The amines cadaverine and putrescine are not substrates [2]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1116448-48-6 |
| References: |
| 1. |
Lucas-Elío, P., Gómez, D., Solano, F. and Sanchez-Amat, A. The antimicrobial activity of marinocine, synthesized by Marinomonas mediterranea, is due to hydrogen peroxide generated by its lysine oxidase activity. J. Bacteriol. 188 (2006) 2493–2501. [DOI] [PMID: 16547036] |
| 2. |
Gómez, D., Lucas-Elío, P., Sanchez-Amat, A. and Solano, F. A novel type of lysine oxidase: L-lysine-ε-oxidase. Biochim. Biophys. Acta 1764 (2006) 1577–1585. [DOI] [PMID: 17030025] |
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| [EC 1.4.3.20 created 2006, modified 2011] |
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