BRENDA - Enzyme Database show
show all sequences of 1.14.13.61

2-Oxo-1,2-dihydroquinoline 8-monooxygenase: phylogenetic relationship to other multicomponent nonheme iron oxygenases

Rosche, B.; Tshisuaka, B.; Hauer, B.; Lingens, F.; Fetzner, S.; J. Bacteriol. 179, 3549-3554 (1997)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Pseudomonas putida
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37000
-
x * 51200, calculation from nucleotide sequence, oxygenase component + x * 37000, calculation from nucleotide sequence, reductase component
Pseudomonas putida
51200
-
x * 51200, calculation from nucleotide sequence, oxygenase component + x * 37000, calculation from nucleotide sequence, reductase component
Pseudomonas putida
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
-
-
Pseudomonas putida 86
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 51200, calculation from nucleotide sequence, oxygenase component + x * 37000, calculation from nucleotide sequence, reductase component
Pseudomonas putida
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Pseudomonas putida
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37000
-
x * 51200, calculation from nucleotide sequence, oxygenase component + x * 37000, calculation from nucleotide sequence, reductase component
Pseudomonas putida
51200
-
x * 51200, calculation from nucleotide sequence, oxygenase component + x * 37000, calculation from nucleotide sequence, reductase component
Pseudomonas putida
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 51200, calculation from nucleotide sequence, oxygenase component + x * 37000, calculation from nucleotide sequence, reductase component
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
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-