BRENDA - Enzyme Database show
show all sequences of 1.14.99.2

Studies on the metabolism of kynurenic acid

Taniuchi, H.; Hayaishi, O.; J. Biol. Chem. 238, 283-293 (1963)

Data extracted from this reference:

General Stability
General Stability
Organism
2-mercaptoethanol stabilizes activity
Pseudomonas fluorescens
cysteine stabilizes activity
Pseudomonas fluorescens
GSH stabilizes activity
Pseudomonas fluorescens
precipitation of supernatant with ammonium sulfate in the absence of cysteine, complete loss of activity
Pseudomonas fluorescens
thioglycolate stabilizes activity
Pseudomonas fluorescens
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ag+
-
Pseudomonas fluorescens
Cu2+
-
Pseudomonas fluorescens
Hg2+
-
Pseudomonas fluorescens
iodoacetate
inhibition reversed by addition of GSH or cysteine
Pseudomonas fluorescens
Kynurenate
competitive inhibition at 0.2 mM
Pseudomonas fluorescens
p-chloromercuribenzoate
inhibition reversed by addition of GSH or cysteine
Pseudomonas fluorescens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.008
-
Kynurenate
-
Pseudomonas fluorescens
0.04
-
NADH
-
Pseudomonas fluorescens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
kynurenate + NADH + O2
Pseudomonas fluorescens
-
7,8-dihydro-7,8-dihydroxykynurenate + NAD+
-
-
?
kynurenate + NADPH + O2
Pseudomonas fluorescens
-
7,8-dihydro-7,8-dihydroxykynurenate + NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas fluorescens
-
ATCC 11299b
-
Purification (Commentary)
Commentary
Organism
partial
Pseudomonas fluorescens
Storage Stability
Storage Stability
Organism
-10C, ammonium sulfate fractions, loss of activity after a few days
Pseudomonas fluorescens
-10C, supernatant after high speed centrifugation of crude extract, several months, no loss in activity
Pseudomonas fluorescens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
kynurenate + NADH + O2
-
390584
Pseudomonas fluorescens
7,8-dihydro-7,8-dihydroxykynurenate + NAD+
-
-
-
?
kynurenate + NADPH + O2
-
390584
Pseudomonas fluorescens
7,8-dihydro-7,8-dihydroxykynurenate + NADP+
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
23
-
assay at
Pseudomonas fluorescens
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
60
-
5 min, complete inactivation
Pseudomonas fluorescens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Pseudomonas fluorescens
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
9
-
stable in presence 10 mM cysteine
Pseudomonas fluorescens
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Pseudomonas fluorescens
NADPH
-
Pseudomonas fluorescens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Pseudomonas fluorescens
NADPH
-
Pseudomonas fluorescens
General Stability (protein specific)
General Stability
Organism
2-mercaptoethanol stabilizes activity
Pseudomonas fluorescens
cysteine stabilizes activity
Pseudomonas fluorescens
GSH stabilizes activity
Pseudomonas fluorescens
precipitation of supernatant with ammonium sulfate in the absence of cysteine, complete loss of activity
Pseudomonas fluorescens
thioglycolate stabilizes activity
Pseudomonas fluorescens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ag+
-
Pseudomonas fluorescens
Cu2+
-
Pseudomonas fluorescens
Hg2+
-
Pseudomonas fluorescens
iodoacetate
inhibition reversed by addition of GSH or cysteine
Pseudomonas fluorescens
Kynurenate
competitive inhibition at 0.2 mM
Pseudomonas fluorescens
p-chloromercuribenzoate
inhibition reversed by addition of GSH or cysteine
Pseudomonas fluorescens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.008
-
Kynurenate
-
Pseudomonas fluorescens
0.04
-
NADH
-
Pseudomonas fluorescens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
kynurenate + NADH + O2
Pseudomonas fluorescens
-
7,8-dihydro-7,8-dihydroxykynurenate + NAD+
-
-
?
kynurenate + NADPH + O2
Pseudomonas fluorescens
-
7,8-dihydro-7,8-dihydroxykynurenate + NADP+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
partial
Pseudomonas fluorescens
Storage Stability (protein specific)
Storage Stability
Organism
-10C, ammonium sulfate fractions, loss of activity after a few days
Pseudomonas fluorescens
-10C, supernatant after high speed centrifugation of crude extract, several months, no loss in activity
Pseudomonas fluorescens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
kynurenate + NADH + O2
-
390584
Pseudomonas fluorescens
7,8-dihydro-7,8-dihydroxykynurenate + NAD+
-
-
-
?
kynurenate + NADPH + O2
-
390584
Pseudomonas fluorescens
7,8-dihydro-7,8-dihydroxykynurenate + NADP+
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
23
-
assay at
Pseudomonas fluorescens
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
60
-
5 min, complete inactivation
Pseudomonas fluorescens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Pseudomonas fluorescens
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
9
-
stable in presence 10 mM cysteine
Pseudomonas fluorescens
Other publictions for EC 1.14.99.2
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)
396602
Gibson
-
Assay of enzymes of aromatic m ...
Pseudomonas sp.
Methods Microbiol.
6A
463-478
1971
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390584
Taniuchi
Studies on the metabolism of k ...
Pseudomonas fluorescens
J. Biol. Chem.
238
283-293
1963
-
-
-
-
-
5
6
2
-
-
-
2
-
1
-
-
1
-
-
-
-
2
2
-
1
-
1
-
1
-
1
2
-
-
-
-
-
-
2
-
-
5
-
6
-
2
-
-
-
2
-
-
-
1
-
-
-
2
2
-
1
-
1
-
1
-
1
-
-
-
-
-
-
-