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In enzymology, a 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase (EC 1.13.11.48) is an enzyme that catalyzes the chemical reaction

3-hydroxy-2-methyl-1H-quinolin-4-one + O₂ ${\displaystyle \rightleftharpoons }$ N-acetylanthranilate + CO

Thus, the two substrates of this enzyme are 3-hydroxy-2-methyl-1H-quinolin-4-one and O₂, whereas its two products are N-acetylanthranilate 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-2-methyl-1H-quinolin-4-one 2,4-dioxygenase (CO-forming). This enzyme is also called (1H)-3-hydroxy-4-oxoquinaldine 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.

• Biology

• EC 1.13.11
• Enzymes of unknown structure