EC 1.4.3.20 - L-lysine 6-oxidase

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IntEnz Enzyme Nomenclature
EC 1.4.3.20

Names

Accepted name:
L-lysine 6-oxidase
Other names:
L-lysine-ε-oxidase
Lod
LodA
marinocine
Systematic name:
L-lysine:oxygen 6-oxidoreductase (deaminating)

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033736
UniProtKB/Swiss-Prot:

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: 2493-2501 (2006). [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: 1577-1585 (2006). [PMID: 17030025]

[EC 1.4.3.20 created 2006, modified 2011]