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3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase

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-methylquinolin-4-one 2,4-dioxygenase
Identifiers
EC no.1.13.11.48
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins
3-hydroxy-2-methyl-1H-quinolin-4-one + O2 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 edit

  • 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.

hydroxy, methylquinolin, dioxygenase, enzymology, enzyme, that, catalyzes, chemical, reactionidentifiersec, 48databasesintenzintenz, viewbrendabrenda, entryexpasynicezyme, viewkeggkegg, entrymetacycmetabolic, pathwaypriamprofilepdb, structuresrcsb, pdbe, pdbsu. In enzymology a 3 hydroxy 2 methylquinolin 4 one 2 4 dioxygenase EC 1 13 11 48 is an enzyme that catalyzes the chemical reaction3 hydroxy 2 methylquinolin 4 one 2 4 dioxygenaseIdentifiersEC no 1 13 11 48DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteins 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 editBauer 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 Portal nbsp Biology Retrieved from https en wikipedia org w index php title 3 hydroxy 2 methylquinolin 4 one 2 4 dioxygenase amp oldid 1172335665, wikipedia, wiki, book, books, library,

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