Lysine 2-monooxygenase

Lysine 2-monooxygenase
Identifiers
EC no.1.13.12.2
CAS no.9031-22-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Lysine 2-monooxygenase (EC 1.13.12.2) is an enzyme that catalyzes the chemical reaction

 
O2
CO2 + H2O
 
 
 
5-aminopentanamide

The two substrates of this enzyme are L-lysine and oxygen. Its products are 5-aminopentanamide, carbon dioxide, and water.[1][2][3]

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O with incorporation of one atom of oxygen (internal monooxygenases o internal mixed-function oxidases). The systematic name of this enzyme class is L-lysine:oxygen 2-oxidoreductase (decarboxylating). Other names in common use include lysine oxygenase, lysine monooxygenase, and L-lysine-2-monooxygenase. This enzyme participates in lysine degradation. It employs one cofactor, flavin adenine dinucleotide.[4]

References

  1. ^ Enzyme 1.13.12.2 at KEGG Pathway Database.
  2. ^ Takeda H, Hayaishi O (1966). "Crystalline L-lysine oxygenase". J. Biol. Chem. 241 (11): 2733–6. doi:10.1016/S0021-9258(18)96601-9. PMID 5911646.
  3. ^ Takeda H, Yamamoto S, Kojima Y, Hayaishi O (1969). "Studies on monooxygenases. I. General properties of crystalline L-lysine monooxygenase". J. Biol. Chem. 244 (11): 2935–41. doi:10.1016/S0021-9258(18)91714-X. PMID 5772467.
  4. ^ Nakazawa T, Hori K, Hayaishi O (1972). "Studies on monooxygenases. V. Manifestation of amino acid oxidase activity by L-lysine monooxygenase". J. Biol. Chem. 247 (11): 3439–44. doi:10.1016/S0021-9258(19)45160-0. PMID 4624115.