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

In enzymology, a 3-hydroxy-4-oxoquinoline 2,4-dioxygenase (EC 1.13.11.47) is an enzyme that catalyzes the chemical reaction

3-hydroxy-1H-quinolin-4-one + O2 N-formylanthranilate + CO
3-hydroxy-4-oxoquinoline 2,4-dioxygenase
Identifiers
EC number1.13.11.47
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are 3-hydroxy-1H-quinolin-4-one and O2, whereas its two products are N-formylanthranilate and CO.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 3-hydroxy-1H-quinolin-4-one 2,4-dioxygenase (CO-forming). Other names in common use include (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, and quinoline-3,4-diol 2,4-dioxygenase.

References
    • Bauer I, De Beyer A, Tsisuaka B, Fetzner S, Lingens F (1994). "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 (3): 299–304. doi:10.1111/j.1574-6968.1994.tb06783.x.
    • Bauer I, Max N, Fetzner S, Lingens F (1996). "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 (3): 576–83. doi:10.1111/j.1432-1033.1996.0576h.x. PMID 8856057.
    • Fischer F, Kunne S, Fetzner S (1999). "Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases". J. Bacteriol. 181 (18): 5725–33. PMC 94093. PMID 10482514.
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