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Information on EC 1.14.13.61 - 2-hydroxyquinoline 8-monooxygenase
for references in articles please use BRENDA:EC1.14.13.61
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
1.14.13.61 2-hydroxyquinoline 8-monooxygenase
IUBMB Comments
Requires iron. Quinolin-2-ol exists largely as the quinolin-2(1H)-one tautomer.
The enzyme appears in viruses and cellular organisms
- 1.14.13.61
- putida
-
multicomponent
- oxygenases
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two-component
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iron-sulfur
- flavin
- flavoprotein
-
rieske-type
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nadh-dependent
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rieske
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non-heme
showSynonyms
2-oxo-1,2-dihydroquinoline 8-monooxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-oxo-1,2-dihydroquinoline 8-monooxygenase
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-
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2-oxo-1,2-dihydroquinoline 8-monooxygenase (Pseudomonas putida strain 86 gene oxoO subunit)
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-
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2-oxo-1,2-dihydroquinoline 8-monooxygenase (Pseudomonas putida strain 86 gene oxoR subunit)
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-
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2-oxoquinoline 8-monooxygenase oxygenase
GenBank Y12654-derived protein GI 2072729
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GenBank Y12655-derived protein GI 2072732
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-
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OMO
Oxygenase, 2-oxo-1,2-dihydroquinoline 8-mono-
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Oxygenase, 2-oxo-1,2-dihydroquinoline 8-mono- (Pseudomonas putida strain 86 gene oxoO subunit)
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Oxygenase, 2-oxo-1,2-dihydroquinoline 8-mono- (Pseudomonas putida strain 86 gene oxoR subunit)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
quinolin-2-ol + NADH + H+ + O2 = quinolin-2,8-diol + NAD+ + H2O
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-
-
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quinolin-2-ol + NADH + H+ + O2 = quinolin-2,8-diol + NAD+ + H2O
active site modulation by Rieske-[2Fe-2S] center oxidation/reduction
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quinolin-2-ol + NADH + H+ + O2 = quinolin-2,8-diol + NAD+ + H2O
active site modulation by Rieske-[2Fe-2S] center oxidation/reduction
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
quinolin-2(1H)-one,NADH:oxygen oxidoreductase (8-oxygenating)
Requires iron. Quinolin-2-ol exists largely as the quinolin-2(1H)-one tautomer.
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CAS REGISTRY NUMBER
COMMENTARY
166799-89-9
-
191941-72-7
GenBank Y12655-derived protein GI 2072732, 2-oxo-1,2-dihydroquinoline 8-monooxygenase (Pseudomonas putida strain 86 gene oxoR subunit)
191941-74-9
GenBank Y12655-derived protein GI, 2-oxo-1,2-dihydroquinoline 8-monooxygenase (Pseudomonas putida strain 86 gene oxoO subunit)
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-Oxo-1,2-dihydroquinoline + NADH + O2
8-Hydroxy-2-oxo-1,2-dihydroquinoline + NAD+ + H2O
-
Substrates: no catalytic activity under anaerobic conditions
Products: -
Products: -
?
2-Oxo-1,2-dihydroquinoline + NADH + O2
8-Hydroxy-2-oxo-1,2-dihydroquinoline + NAD+ + H2O
-
Substrates: no catalytic activity under anaerobic conditions
Products: -
Products: -
?
2-Oxo-1,2-dihydroquinoline + NADH + O2
?
-
Substrates: second enzyme in the quinoline degradation pathway. The reductase component and the oxygenase component are inducible by the substrate 2-oxo-1,2-dihydroquinoline
Products: -
Products: -
?
2-Oxo-1,2-dihydroquinoline + NADH + O2
?
-
Substrates: second enzyme in the quinoline degradation pathway. The reductase component and the oxygenase component are inducible by the substrate 2-oxo-1,2-dihydroquinoline
Products: -
Products: -
?
quinolin-2-ol + NADH + O2
quinolin-2,8-diol + NAD+ + H2O
-
Substrates: the N-heteroaromatic compound quinoline acts as sole source of carbon, nitrogen, and energy in the aerobic soil bacterium
Products: -
Products: -
?
quinolin-2-ol + NADH + O2
quinolin-2,8-diol + NAD+ + H2O
-
Substrates: the mononuclear Fe2+ ion and can open a pathway for dioxygen to bind in the substrate-containing active site, substrate binding structure, overview
Products: -
Products: -
?
quinolin-2-ol + NADH + O2
quinolin-2,8-diol + NAD+ + H2O
-
Substrates: the N-heteroaromatic compound quinoline acts as sole source of carbon, nitrogen, and energy in the aerobic soil bacterium
Products: -
Products: -
?
quinolin-2-ol + NADH + O2
quinolin-2,8-diol + NAD+ + H2O
-
Substrates: the mononuclear Fe2+ ion and can open a pathway for dioxygen to bind in the substrate-containing active site, substrate binding structure, overview
Products: -
Products: -
?
additional information
?
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Substrates: the reductase component shows NADH:acceptor reductase activity with: cytochrome c, ferricyanide, 2,6-dichlorophenol indophenol and 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyl-2H-tetrazolium chloride
Products: -
Products: -
?
additional information
?
-
-
Substrates: the reductase component shows NADH:acceptor reductase activity with: cytochrome c, ferricyanide, 2,6-dichlorophenol indophenol and 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyl-2H-tetrazolium chloride
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-Oxo-1,2-dihydroquinoline + NADH + O2
?
-
Substrates: second enzyme in the quinoline degradation pathway. The reductase component and the oxygenase component are inducible by the substrate 2-oxo-1,2-dihydroquinoline
Products: -
Products: -
?
2-Oxo-1,2-dihydroquinoline + NADH + O2
?
-
Substrates: second enzyme in the quinoline degradation pathway. The reductase component and the oxygenase component are inducible by the substrate 2-oxo-1,2-dihydroquinoline
Products: -
Products: -
?
quinolin-2-ol + NADH + O2
quinolin-2,8-diol + NAD+ + H2O
-
Substrates: the N-heteroaromatic compound quinoline acts as sole source of carbon, nitrogen, and energy in the aerobic soil bacterium
Products: -
Products: -
?
quinolin-2-ol + NADH + O2
quinolin-2,8-diol + NAD+ + H2O
-
Substrates: the N-heteroaromatic compound quinoline acts as sole source of carbon, nitrogen, and energy in the aerobic soil bacterium
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Fe2+
-
the enzyme is a Rieske non-heme iron oxygenase, an active site Rieske-[2Fe-2S] center is involved in the enzyme complex, structure analysis of oxidized, reduced, and substrate bound states, overview
Iron
-
the reductase component contains 1 plant-type ferredoxin [2Fe-2S] cluster, the oxygenase component contains 6 Rieske-type [2Fe-2S]clusters and additional iron
Iron
-
the oxygenase component is a Rieske [2Fe-2S]protein, the reductase component contains a [2Fe-2S]cluster. Study of the 2Fe-2S centres by EPR spectroscopy
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37000
51200
-
x * 51200, calculation from nucleotide sequence, oxygenase component + x * 37000, calculation from nucleotide sequence, reductase component
55000
-
the reductase component is a monomer, 1 * 37000, SDS-PAGE. The oxygenase component is a hexamer, 6 * 55000, SDS-PAGE
37000
-
x * 51200, calculation from nucleotide sequence, oxygenase component + x * 37000, calculation from nucleotide sequence, reductase component
37000
-
the reductase component is a monomer, 1 * 37000, SDS-PAGE. The oxygenase component is a hexamer, 6 * 55000, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 51200, calculation from nucleotide sequence, oxygenase component + x * 37000, calculation from nucleotide sequence, reductase component
?
-
the reductase component is a monomer, 1 * 37000, SDS-PAGE. The oxygenase component is a hexamer, 6 * 55000, SDS-PAGE
?
-
the reductase component is a monomer, 1 * 37000, SDS-PAGE. The oxygenase component is a hexamer, 6 * 55000, SDS-PAGE
-
?
-
x * 51200, calculation from nucleotide sequence, oxygenase component + x * 37000, calculation from nucleotide sequence, reductase component
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additional information
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detailed enzyme structure analysis in oxidized, reduced, and substrate bound states, from cyrstal structure, overview
additional information
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detailed enzyme structure analysis in oxidized, reduced, and substrate bound states, from cyrstal structure, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme, hanging drop vapour diffusion method, 50 mg/ml protein in 10 mM Tris-HCl, pH 8.0, is mixed with reservoir solution, containing 3335% PEG 400, 200 mM ammonium tartrate, pH 6.5, in a 3:2 ratio with a resulting pH of 7.0, at aerobic conditions, 3 days at 17°C, under anaerobic conditions a reservoir solution containing 2930% PEG 400, 200 mM ammonium tartrate, 5 mM Na-dithionite, pH 6.5, is mixed with protein reduced by 5 mM Na-dithionite in a ratio of 2:2 at 15°C, X-ray diffraction structure determination and analysis at 2.5 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by ion exchange and hydrophobic interaction chromatography, and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rosche, B.; Tshisuaka, B.; Fetzner, S.; Lingens, F.
2-Oxo-1,2-dihydroquinoline 8-monooxygenase,a two-component enzyme system from Pseudomonas putida 86
J. Biol. Chem.
270
17836-17842
1995
Pseudomonas putida, Pseudomonas putida 86
brenda
Rosche, B.; Tshisuaka, B.; Hauer, B.; Lingens, F.; Fetzner, S.
2-Oxo-1,2-dihydroquinoline 8-monooxygenase: phylogenetic relationship to other multicomponent nonheme iron oxygenases
J. Bacteriol.
179
3549-3554
1997
Pseudomonas putida, Pseudomonas putida 86
brenda
Rosche, B.; Fetzner, S.; Lingens, F.; Nitschke, W.; Riedel, A.
The 2Fe2S centres of the 2-oxo-1,2-dihydroquinoline 8-monooxygenase from Pseudomonas putida 86 studied by EPR spectroscopy
Biochim. Biophys. Acta
1252
177-179
1995
Pseudomonas putida, Pseudomonas putida 86
brenda
Martins, B.M.; Svetlitchnaia, T.; Dobbek, H.
2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction
Structure
13
817-824
2005
Pseudomonas putida, Pseudomonas putida 86
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.13.61)
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Release 2023.1 (January 2023)
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