Reaction: 3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO
For diagram click here.
Other name(s): (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase
Systematic name: 3-hydroxy-2-methyl-1H-quinolin-4-one 2,4-dioxygenase (CO-forming)
Comments: 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 22.214.171.124, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase), but more slowly.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 160995-63-1
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 1H-3-hydroxy-4-oxoquinoline. FEMS Microbiol. Lett. 117 (1994) 299-304.
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 1H-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 (1996) 576-583. [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 (1999) 5725-5733. [PMID: 10482514]