View source for 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase

{{Short description|Class of enzymes}}
{{infobox enzyme
| Name       = 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
| EC_number  = 1.13.11.48
| CAS_number =
| GO_code    = 0050586
| image      =
| width      =
| caption    =
}}
In [[enzymology]], a '''3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase''' ({{EC number|1.13.11.48}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
:3-hydroxy-2-methyl-1H-quinolin-4-one + O<sub>2</sub> <math>\rightleftharpoons</math> N-acetylanthranilate + CO
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[3-hydroxy-2-methyl-1H-quinolin-4-one]] and [[oxygen|O<sub>2</sub>]], whereas its two [[product (chemistry)|products]] are [[N-acetylanthranilate]] and [[carbon monoxide|CO]].
This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on single donors with O<sub>2</sub> as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O<sub>2</sub>.  The [[List of enzymes|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==
{{reflist|1}}
* {{cite journal | vauthors = Bauer I, De Beyer A, Tsisuaka B, Fetzner S, Lingens F | date = 1994 | title = A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline | journal = FEMS Microbiol. Lett.  | volume = 117 | issue = 3 | pages = 299–304 | doi = 10.1111/j.1574-6968.1994.tb06783.x | doi-access = free }}
* {{cite journal | doi = 10.1111/j.1432-1033.1996.0576h.x | vauthors = Bauer I, Max N, Fetzner S, Lingens F | date = 1996 | title = 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 | journal = Eur. J. Biochem.  | volume = 240 | pages = 576–83  | pmid = 8856057 | issue = 3 | doi-access = free }}
* {{cite journal | vauthors = Fischer F, Kunne S, Fetzner S | date = 1999 | title = Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases | journal = J. Bacteriol.  | volume = 181 | pages = 5725–33  | pmid = 10482514 | issue = 18 | pmc = 94093 }}
{{Monooxygenases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}
[[Category:EC 1.13.11]]
[[Category:Enzymes of unknown structure]]