BRENDA - Enzyme Database
show all sequences of 1.14.12.16

Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase from Comamonas testosteroni 63. The first two enzymes in quinoline and 3-methylquinoline degradation

Schach, S.; Tshisuaka, B.; Fetzner, S.; Lingens, F.; Eur. J. Biochem. 232, 536-544 (1995)

Data extracted from this reference:

General Stability
General Stability
Organism
dithioerythritol, dithiothreitol and 2-oxo-1,2-dihydroquinoline stabilize
Comamonas testosteroni
Inhibitors
Inhibitors
Commentary
Organism
Structure
1,10-phenanthroline
0.5 mM, 82% loss of activity
Comamonas testosteroni
4-hydroxymercuribenzoate
0.1 mM, complete loss of activity
Comamonas testosteroni
Acriflavin
0.5 mM, 69% loss of activity
Comamonas testosteroni
Cu2+
-
Comamonas testosteroni
diethyldithiocarbaminate
inhibits after a prolonged incubation time
Comamonas testosteroni
EDTA
inhibits after a prolonged incubation time
Comamonas testosteroni
iodoacetate
2 mM, complete loss of activity
Comamonas testosteroni
NaCl
0.2 M, 50% loss of activity
Comamonas testosteroni
Quinacrine
0.5 mM, 15% loss of activity
Comamonas testosteroni
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
enhances activity 1.5fold
Comamonas testosteroni
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Comamonas testosteroni
second enzyme in the pathway of quinoline and 3-methylquinoline degradation
?
-
-
?
additional information
Comamonas testosteroni 63
second enzyme in the pathway of quinoline and 3-methylquinoline degradation
?
-
-
?
Organic Solvent Stability
Organic Solvent
Commentary
Organism
Ethanol
5%, decreases enzyme activity to 44%
Comamonas testosteroni
Organism
Organism
UniProt
Commentary
Textmining
Comamonas testosteroni
-
-
-
Comamonas testosteroni 63
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
partial
Comamonas testosteroni
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.125
-
-
Comamonas testosteroni
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
2-Oxo-1,2-dihydroquinoline + NADH + O2
-
7068
Comamonas testosteroni
?
-
-
-
?
2-Oxo-1,2-dihydroquinoline + NADH + O2
-
7068
Comamonas testosteroni 63
?
-
-
-
?
3-Methyl-2-oxo-1,2-dihydroquinoline + NADH + O2
NADH cannot be replaced by NADPH
7068
Comamonas testosteroni
5,6-Dihydro-5,6-dihydroxy-(3-methyl-)2-oxo-1,2-dihydroquinoline + NAD+
-
7068
Comamonas testosteroni
?
3-Methyl-2-oxo-1,2-dihydroquinoline + NADH + O2
NADH cannot be replaced by NADPH
7068
Comamonas testosteroni 63
5,6-Dihydro-5,6-dihydroxy-(3-methyl-)2-oxo-1,2-dihydroquinoline + NAD+
-
7068
Comamonas testosteroni 63
?
6-Hydroxy-2-oxo-1,2-dihydroquinoline + NADH + O2
-
7068
Comamonas testosteroni
?
-
-
-
?
6-Hydroxy-2-oxo-1,2-dihydroquinoline + NADH + O2
-
7068
Comamonas testosteroni 63
?
-
-
-
?
8-Hydroxy-2-oxo-1,2-dihydroquinoline + NADH + O2
-
7068
Comamonas testosteroni
?
-
-
-
?
8-Hydroxyquinoline + NADH + O2
-
7068
Comamonas testosteroni
?
-
-
-
?
8-Hydroxyquinoline + NADH + O2
-
7068
Comamonas testosteroni 63
?
-
-
-
?
additional information
second enzyme in the pathway of quinoline and 3-methylquinoline degradation
7068
Comamonas testosteroni
?
-
-
-
?
additional information
second enzyme in the pathway of quinoline and 3-methylquinoline degradation
7068
Comamonas testosteroni 63
?
-
-
-
?
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
-
5 min, 30% loss of activity
Comamonas testosteroni
65
-
5 min, complete loss of activity
Comamonas testosteroni
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
-
Comamonas testosteroni
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
required, cannot be replaced by NADPH
Comamonas testosteroni
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
required, cannot be replaced by NADPH
Comamonas testosteroni
General Stability (protein specific)
General Stability
Organism
dithioerythritol, dithiothreitol and 2-oxo-1,2-dihydroquinoline stabilize
Comamonas testosteroni
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1,10-phenanthroline
0.5 mM, 82% loss of activity
Comamonas testosteroni
4-hydroxymercuribenzoate
0.1 mM, complete loss of activity
Comamonas testosteroni
Acriflavin
0.5 mM, 69% loss of activity
Comamonas testosteroni
Cu2+
-
Comamonas testosteroni
diethyldithiocarbaminate
inhibits after a prolonged incubation time
Comamonas testosteroni
EDTA
inhibits after a prolonged incubation time
Comamonas testosteroni
iodoacetate
2 mM, complete loss of activity
Comamonas testosteroni
NaCl
0.2 M, 50% loss of activity
Comamonas testosteroni
Quinacrine
0.5 mM, 15% loss of activity
Comamonas testosteroni
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
enhances activity 1.5fold
Comamonas testosteroni
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Comamonas testosteroni
second enzyme in the pathway of quinoline and 3-methylquinoline degradation
?
-
-
?
additional information
Comamonas testosteroni 63
second enzyme in the pathway of quinoline and 3-methylquinoline degradation
?
-
-
?
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
Ethanol
5%, decreases enzyme activity to 44%
Comamonas testosteroni
Purification (Commentary) (protein specific)
Commentary
Organism
partial
Comamonas testosteroni
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.125
-
-
Comamonas testosteroni
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
2-Oxo-1,2-dihydroquinoline + NADH + O2
-
7068
Comamonas testosteroni
?
-
-
-
?
2-Oxo-1,2-dihydroquinoline + NADH + O2
-
7068
Comamonas testosteroni 63
?
-
-
-
?
3-Methyl-2-oxo-1,2-dihydroquinoline + NADH + O2
NADH cannot be replaced by NADPH
7068
Comamonas testosteroni
5,6-Dihydro-5,6-dihydroxy-(3-methyl-)2-oxo-1,2-dihydroquinoline + NAD+
-
7068
Comamonas testosteroni
?
3-Methyl-2-oxo-1,2-dihydroquinoline + NADH + O2
NADH cannot be replaced by NADPH
7068
Comamonas testosteroni 63
5,6-Dihydro-5,6-dihydroxy-(3-methyl-)2-oxo-1,2-dihydroquinoline + NAD+
-
7068
Comamonas testosteroni 63
?
6-Hydroxy-2-oxo-1,2-dihydroquinoline + NADH + O2
-
7068
Comamonas testosteroni
?
-
-
-
?
6-Hydroxy-2-oxo-1,2-dihydroquinoline + NADH + O2
-
7068
Comamonas testosteroni 63
?
-
-
-
?
8-Hydroxy-2-oxo-1,2-dihydroquinoline + NADH + O2
-
7068
Comamonas testosteroni
?
-
-
-
?
8-Hydroxyquinoline + NADH + O2
-
7068
Comamonas testosteroni
?
-
-
-
?
8-Hydroxyquinoline + NADH + O2
-
7068
Comamonas testosteroni 63
?
-
-
-
?
additional information
second enzyme in the pathway of quinoline and 3-methylquinoline degradation
7068
Comamonas testosteroni
?
-
-
-
?
additional information
second enzyme in the pathway of quinoline and 3-methylquinoline degradation
7068
Comamonas testosteroni 63
?
-
-
-
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
-
5 min, 30% loss of activity
Comamonas testosteroni
65
-
5 min, complete loss of activity
Comamonas testosteroni
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
-
Comamonas testosteroni
Other publictions for EC 1.14.12.16
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
Synonyms
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)
7068
Schach
Quinoline 2-oxidoreductase and ...
Comamonas testosteroni, Comamonas testosteroni 63
Eur. J. Biochem.
232
536-544
1995
-
-
-
-
-
1
9
-
-
1
-
2
1
9
-
-
1
-
-
-
1
-
11
-
-
-
-
2
-
1
-
-
1
-
-
-
-
-
-
1
-
-
1
-
9
-
-
-
1
-
2
1
-
-
1
-
-
1
-
11
-
-
-
2
-
1
-
-
-
-
-
-
-
-
-