Accepted name: 3-hydroxy-4-oxoquinoline 2,4-dioxygenase
Reaction: 3-hydroxy-1H-quinolin-4-one + O2 = N-formylanthranilate + CO
Other name(s): (1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase; 3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase; 3-hydroxy-4(1H)-one, 2,4-dioxygenase; quinoline-3,4-diol 2,4-dioxygenase
Systematic name: 3-hydroxy-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 Pseudomonas putida is highly specific for this substrate.
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 hydrolase-fold superfamily of enzymes functionally related to serine hydrolases. J. Bacteriol. 181 (1999) 5725–5733. [PMID: 10482514]
[EC created 1999 as EC, transferred 2001 to EC (EC created 1999 deleted 2001 as identical)]