EC - 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
Other name:
(1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase
Systematic name:
3-hydroxy-2-methyl-1H-quinolin-4-one 2,4-dioxygenase (CO-forming)



Does not contain a metal centre or organic cofactor. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. The enzyme from Arthrobacter sp. can also act on 3-hydroxy-4-oxoquinoline, forming N-formylanthranilate and CO (cf. EC, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase), but more slowly.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050586


  1. Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S. and Lingens, F.
    A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1 H-3-hydroxy-4-oxoquinoline.
    FEMS Microbiol. Lett. 117 : 299-304 (1994).
  2. Bauer, I., Max, N., Fetzner, S. and Lingens, F.
    2,4-Dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1 H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1.
    Eur. J. Biochem. 240 : 576-583 (1996). [PMID: 8856057]
  3. Fischer, F., Kunne, S. and Fetzner, S.
    Bacterial 2,4-dioxygenases: new members of the α/β hydrolase-fold superfamily of enzymes functionally related to serine hydrolases.
    J. Bacteriol. 181 : 5725-5733 (1999). [PMID: 10482514]

[EC created 2001]