KEGG   ENZYME: 1.4.3.20Help
Entry
EC 1.4.3.20                 Enzyme                                 

Name
L-lysine 6-oxidase;
L-lysine-epsilon-oxidase;
Lod;
LodA;
marinocine
Class
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
L-lysine:oxygen 6-oxidoreductase (deaminating)
Reaction(IUBMB)
L-lysine + O2 + H2O = (S)-2-amino-6-oxohexanoate + H2O2 + NH3 [RN:R07598]
Reaction(KEGG)
Substrate
L-lysine [CPD:C00047];
O2 [CPD:C00007];
H2O [CPD:C00001]
Product
(S)-2-amino-6-oxohexanoate [CPD:C04076];
H2O2 [CPD:C00027];
NH3 [CPD:C00014]
Comment
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].
History
EC 1.4.3.20 created 2006, modified 2011
Orthology
K17831  
L-lysine 6-oxidase
Genes
MMW: 
MME: 
Taxonomy
Reference
1  [PMID:16547036]
  Authors
Lucas-Elio P, Gomez D, Solano F, Sanchez-Amat A.
  Title
The antimicrobial activity of marinocine, synthesized by Marinomonas mediterranea, is due to hydrogen peroxide generated by its lysine oxidase activity.
  Journal
J. Bacteriol. 188 (2006) 2493-501.
  Organism
Marinomonas mediterranea [GN:mme]
  Sequence
Reference
2  [PMID:17030025]
  Authors
Gomez D, Lucas-Elio P, Sanchez-Amat A, Solano F.
  Title
A novel type of lysine oxidase: L-lysine-epsilon-oxidase.
  Journal
Biochim. Biophys. Acta. 1764 (2006) 1577-85.
  Organism
Marinomonas mediterranea [GN:mme]
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
1116448-48-6

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