EC 1.13 - Acting on single donors with incorporation of molecular oxygen (oxygenases). The oxygen incorporated need not be derived from O2
EC 188.8.131.52 - 3-hydroxy-4-oxoquinoline 2,4-dioxygenase
IntEnz Enzyme Nomenclature
17949 [IUBMB]3-hydroxy-1H-quinolin-4-one3-hydroxy-1H-quinolin-4-oneName origin: UniProt - CHECKED (C)Formula: C9H7NO2
Charge: 0ChEBI compound status: CHECKED (C)O2O2Name origin: UniProt - CHECKED (C)Formula: O2
Charge: 0ChEBI compound status: CHECKED (C)=COCOName origin: UniProt - CHECKED (C)Formula: CO
Charge: 0ChEBI compound status: CHECKED (C)H+H(+)Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)
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
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).
2,4-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]
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 184.108.40.206 created 1999 as EC 220.127.116.11, transferred 2001 to EC 18.104.22.168 (EC 22.214.171.124 created 1999 deleted 2001 as identical)]