BRENDA - Enzyme Database show
show all sequences of 1.14.13.61

2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction

Martins, B.M.; Svetlitchnaia, T.; Dobbek, H.; Structure 13, 817-824 (2005)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
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 33–35% 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 29–30% 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
Pseudomonas putida
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
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
Pseudomonas putida
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
quinolin-2-ol + NADH + O2
Pseudomonas putida
the N-heteroaromatic compound quinoline acts as sole source of carbon, nitrogen, and energy in the aerobic soil bacterium
quinolin-2,8-diol + NAD+ + H2O
-
-
?
quinolin-2-ol + NADH + O2
Pseudomonas putida 86
the N-heteroaromatic compound quinoline acts as sole source of carbon, nitrogen, and energy in the aerobic soil bacterium
quinolin-2,8-diol + NAD+ + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
-
-
Pseudomonas putida 86
-
-
-
Purification (Commentary)
Commentary
Organism
native enzyme by ion exchange and hydrophobic interaction chromatography, and gel filtration
Pseudomonas putida
Reaction
Reaction
Commentary
Organism
quinolin-2-ol + NADH + H+ + O2 = quinolin-2,8-diol + NAD+ + H2O
active site modulation by Rieske-[2Fe-2S] center oxidation/reduction
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
quinolin-2-ol + NADH + O2
the N-heteroaromatic compound quinoline acts as sole source of carbon, nitrogen, and energy in the aerobic soil bacterium
677152
Pseudomonas putida
quinolin-2,8-diol + NAD+ + H2O
-
-
-
?
quinolin-2-ol + NADH + O2
the mononuclear Fe2+ ion and can open a pathway for dioxygen to bind in the substrate-containing active site, substrate binding structure, overview
677152
Pseudomonas putida
quinolin-2,8-diol + NAD+ + H2O
-
-
-
?
quinolin-2-ol + NADH + O2
the N-heteroaromatic compound quinoline acts as sole source of carbon, nitrogen, and energy in the aerobic soil bacterium
677152
Pseudomonas putida 86
quinolin-2,8-diol + NAD+ + H2O
-
-
-
?
quinolin-2-ol + NADH + O2
the mononuclear Fe2+ ion and can open a pathway for dioxygen to bind in the substrate-containing active site, substrate binding structure, overview
677152
Pseudomonas putida 86
quinolin-2,8-diol + NAD+ + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
detailed enzyme structure analysis in oxidized, reduced, and substrate bound states, from cyrstal structure, overview
Pseudomonas putida
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Pseudomonas putida
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Pseudomonas putida
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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 33–35% 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 29–30% 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
Pseudomonas putida
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
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
Pseudomonas putida
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
quinolin-2-ol + NADH + O2
Pseudomonas putida
the N-heteroaromatic compound quinoline acts as sole source of carbon, nitrogen, and energy in the aerobic soil bacterium
quinolin-2,8-diol + NAD+ + H2O
-
-
?
quinolin-2-ol + NADH + O2
Pseudomonas putida 86
the N-heteroaromatic compound quinoline acts as sole source of carbon, nitrogen, and energy in the aerobic soil bacterium
quinolin-2,8-diol + NAD+ + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme by ion exchange and hydrophobic interaction chromatography, and gel filtration
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
quinolin-2-ol + NADH + O2
the N-heteroaromatic compound quinoline acts as sole source of carbon, nitrogen, and energy in the aerobic soil bacterium
677152
Pseudomonas putida
quinolin-2,8-diol + NAD+ + H2O
-
-
-
?
quinolin-2-ol + NADH + O2
the mononuclear Fe2+ ion and can open a pathway for dioxygen to bind in the substrate-containing active site, substrate binding structure, overview
677152
Pseudomonas putida
quinolin-2,8-diol + NAD+ + H2O
-
-
-
?
quinolin-2-ol + NADH + O2
the N-heteroaromatic compound quinoline acts as sole source of carbon, nitrogen, and energy in the aerobic soil bacterium
677152
Pseudomonas putida 86
quinolin-2,8-diol + NAD+ + H2O
-
-
-
?
quinolin-2-ol + NADH + O2
the mononuclear Fe2+ ion and can open a pathway for dioxygen to bind in the substrate-containing active site, substrate binding structure, overview
677152
Pseudomonas putida 86
quinolin-2,8-diol + NAD+ + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
detailed enzyme structure analysis in oxidized, reduced, and substrate bound states, from cyrstal structure, overview
Pseudomonas putida
Other publictions for EC 1.14.13.61
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
677152
Martins
2-Oxoquinoline 8-monooxygenase ...
Pseudomonas putida, Pseudomonas putida 86
Structure
13
817-824
2005
-
-
-
1
-
-
-
-
-
1
-
2
-
16
-
-
1
1
-
-
-
-
4
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7421
Rosche
2-Oxo-1,2-dihydroquinoline 8-m ...
Pseudomonas putida 86, Pseudomonas putida
J. Bacteriol.
179
3549-3554
1997
-
-
1
-
-
-
-
-
-
-
2
-
-
16
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7420
Rosche
2-Oxo-1,2-dihydroquinoline 8-m ...
Pseudomonas putida, Pseudomonas putida 86
J. Biol. Chem.
270
17836-17842
1995
1
-
-
-
-
-
6
-
-
2
4
2
-
16
-
-
1
-
-
-
2
-
6
1
1
-
-
-
1
-
-
1
-
-
-
1
-
-
1
-
-
-
-
6
-
-
-
2
4
2
-
-
-
1
-
-
2
-
6
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
7422
Rosche
The 2Fe2S centres of the 2-oxo ...
Pseudomonas putida, Pseudomonas putida 86
Biochim. Biophys. Acta
1252
177-179
1995
-
-
-
-
-
-
-
-
-
1
-
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-