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Reference on EC 1.13.11.47 - 3-hydroxy-4-oxoquinoline 2,4-dioxygenase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bauer, I.; Max, N.; Fetzner, S.; Lingens, F.
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. Rii61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1
Eur. J. Biochem.
240
576-583
1996
Arthrobacter sp., Pseudomonas putida, Pseudomonas putida 33/1, Arthrobacter sp. Ru61a
Manually annotated by BRENDA team
Bauer, I.; de Beyer, A.; Tshisuaka, B.; Fetzner, S.; Lingens, F.
A novel type of oxygenolytic ring cleavage: 2,4-oxygenation and decarboxylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline
FEMS Microbiol. Lett.
117
299-304
1994
Pseudomonas putida
-
Manually annotated by BRENDA team
Block, D.W.; Lingens, F.
Microbial metabolism of quinoline and related compounds. XIV. Purification and properties of 1H-3-hydroxy-4-oxoquinoline oxygenase, a new extradiol cleavage enzyme from Pseudomonas putida strain 33/1
Biol. Chem. Hoppe-Seyler
373
343-349
1992
Pseudomonas putida
Manually annotated by BRENDA team
Qi, R.; Fetzner, S.; Oakley, A.J.
Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha/beta-hydrolase family
Acta Crystallogr. Sect. F
63
378-381
2007
Pseudomonas putida, Pseudomonas putida 33/1
Manually annotated by BRENDA team
Steiner, R.A.; Janssen, H.J.; Roversi, P.; Oakley, A.J.; Fetzner, S.
Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold
Proc. Natl. Acad. Sci. USA
107
657-662
2010
Paenarthrobacter nitroguajacolicus (O31266), Paenarthrobacter nitroguajacolicus, Pseudomonas putida (O33472), Pseudomonas putida 33/1 (O33472), Pseudomonas putida 33/1, Paenarthrobacter nitroguajacolicus R61a (O31266)
Manually annotated by BRENDA team
Pietra, F.
Binding pockets and permeation channels for dioxygen through cofactorless 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase in association with its natural substrate, 3-hydroxy-2-methylquinolin-4(1H)-one. A perspective from molecular dynamics simulations
Chem. Biodivers.
11
861-871
2014
Paenarthrobacter nitroguajacolicus (O31266)
Manually annotated by BRENDA team
Hernandez-Ortega, A.; Quesne, M.G.; Bui, S.; Heuts, D.P.; Steiner, R.A.; Heyes, D.J.; de Visser, S.P.; Scrutton, N.S.
Origin of the proton-transfer step in the cofactor-free (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase effect of the basicity of an active site His residue
J. Biol. Chem.
289
8620-8632
2014
Paenarthrobacter nitroguajacolicus (O31266)
Manually annotated by BRENDA team