3-hydroxy-4-oxoquinoline 2,4-dioxygenase;
(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

Oxidoreductases;
Acting on single donors with O2 as oxidant and incorporation of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2;
With incorporation of two atoms of oxygen

3-hydroxy-1H-quinolin-4-one 2,4-dioxygenase (CO-forming)

3-hydroxy-1H-quinolin-4-one + O2 = N-formylanthranilate + CO [RN:R05719]

R05719;
(other) R04915

3-hydroxy-1H-quinolin-4-one [CPD:C11503];
O2 [CPD:C00007]

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  [PMID:8856057]

Bauer I, Max N, Fetzner S, 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) 576-83.

Pseudomonas putida

3  [PMID:10482514]

Fischer F, Kunne S, Fetzner S.

Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases.

J. Bacteriol. 181 (1999) 5725-33.

Pseudomonas putida