The Enzyme Database

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Accepted name: 3-hydroxy-4-oxoquinoline 2,4-dioxygenase
Reaction: 3-hydroxy-1H-quinolin-4-one + O2 = N-formylanthranilate + CO
For diagram of reaction, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 238093-32-8
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. [DOI] [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)]

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