BRENDA - Enzyme Database
show all sequences of 1.14.13.9

Analysis of the wild-type and mutant genes encoding the enzyme kynurenine monooxygenase of the yellow fever mosquito, Aedes aegypti

Han, Q.; Calvo, E.; Marinotti, O.; Fang, J.; Rizzi, M.; James, A.A.; Li, J.; Insect Mol. Biol. 12, 483-490 (2003)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene kh, DNA and amino acid sequence analysis of wild-type and mutant genes, expression in Spodoptera frugiperda Sf9 cells as His-tagged, soluble protein via the baculovirus infection system
Aedes aegypti
Engineering
Protein Variants
Commentary
Organism
additional information
an inactive mutant lacks 162 nucleotides near the 3'-end of the mutant allele, the in-frame deletion results in loss of 54 amino acids leading to loss of enzyme activity and white eyes
Aedes aegypti
Inhibitors
Inhibitors
Commentary
Organism
Structure
chloride
mixed-type inhibition
Aedes aegypti
pyridoxal 5'-phosphate
noncompetitive
Aedes aegypti
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics
Aedes aegypti
0.82
-
NADPH
recombinant enzyme, pH 7.5, 37°C
Aedes aegypti
0.89
-
L-kynurenine
recombinant enzyme, pH 7.5, 37°C
Aedes aegypti
5.17
-
NADH
recombinant enzyme, pH 7.5, 37°C
Aedes aegypti
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
enzyme is hydrophobis and contains 2 transmembrane segments
Aedes aegypti
16020
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
54000
-
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE
Aedes aegypti
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-kynurenine + NADPH + O2
Aedes aegypti
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
L-kynurenine + NADPH + O2
Aedes aegypti Liverpool
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Aedes aegypti
Q86PM2
yellow fever mosquito, black-eyed Liverpool strain
-
Aedes aegypti Liverpool
Q86PM2
yellow fever mosquito, black-eyed Liverpool strain
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His-tagged enzyme from soluble fraction of Sf9 insect cells by nickel affinity chromatography
Aedes aegypti
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
L-kynurenine + NADH + H+ + O2
-
658919
Aedes aegypti
3-hydroxy-L-kynurenine + NAD+ + H2O
-
-
-
?
L-kynurenine + NADH + H+ + O2
-
658919
Aedes aegypti Liverpool
3-hydroxy-L-kynurenine + NAD+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
-
658919
Aedes aegypti
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
658919
Aedes aegypti
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
-
658919
Aedes aegypti Liverpool
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
658919
Aedes aegypti Liverpool
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE
Aedes aegypti
Synonyms
Synonyms
Commentary
Organism
KMO
-
Aedes aegypti
kynurenine hydroxylase
-
Aedes aegypti
kynurenine monooxygenase
-
Aedes aegypti
More
the enzyme is a member of the glutathione reductase structural family
Aedes aegypti
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
-
-
Aedes aegypti
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.85
-
NADH
recombinant enzyme, pH 7.5, 37°C
Aedes aegypti
1.88
-
L-kynurenine
recombinant enzyme, pH 7.5, 37°C
Aedes aegypti
2.03
-
NADPH
recombinant enzyme, pH 7.5, 37°C
Aedes aegypti
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Aedes aegypti
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
consensus domain sequence, probably FAD-containing
Aedes aegypti
NADH
low activity, ineffective cofactor
Aedes aegypti
NADPH
highly preferred cofactor with respect to NADH
Aedes aegypti
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.17
-
pyridoxal 5'-phosphate
recombinant enzyme, with respect to NADPH, pH 7.5, 37°C
Aedes aegypti
0.27
-
pyridoxal 5'-phosphate
recombinant enzyme, with respect to L-kynurenine, pH 7.5, 37°C
Aedes aegypti
11.2
-
chloride
recombinant enzyme, with respect to L-kynurenine, pH 7.5, 37°C
Aedes aegypti
24.5
-
chloride
recombinant enzyme, with respect to NADPH, pH 7.5, 37°C
Aedes aegypti
Cloned(Commentary) (protein specific)
Commentary
Organism
gene kh, DNA and amino acid sequence analysis of wild-type and mutant genes, expression in Spodoptera frugiperda Sf9 cells as His-tagged, soluble protein via the baculovirus infection system
Aedes aegypti
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
consensus domain sequence, probably FAD-containing
Aedes aegypti
NADH
low activity, ineffective cofactor
Aedes aegypti
NADPH
highly preferred cofactor with respect to NADH
Aedes aegypti
Engineering (protein specific)
Protein Variants
Commentary
Organism
additional information
an inactive mutant lacks 162 nucleotides near the 3'-end of the mutant allele, the in-frame deletion results in loss of 54 amino acids leading to loss of enzyme activity and white eyes
Aedes aegypti
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
chloride
mixed-type inhibition
Aedes aegypti
pyridoxal 5'-phosphate
noncompetitive
Aedes aegypti
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.17
-
pyridoxal 5'-phosphate
recombinant enzyme, with respect to NADPH, pH 7.5, 37°C
Aedes aegypti
0.27
-
pyridoxal 5'-phosphate
recombinant enzyme, with respect to L-kynurenine, pH 7.5, 37°C
Aedes aegypti
11.2
-
chloride
recombinant enzyme, with respect to L-kynurenine, pH 7.5, 37°C
Aedes aegypti
24.5
-
chloride
recombinant enzyme, with respect to NADPH, pH 7.5, 37°C
Aedes aegypti
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics
Aedes aegypti
0.82
-
NADPH
recombinant enzyme, pH 7.5, 37°C
Aedes aegypti
0.89
-
L-kynurenine
recombinant enzyme, pH 7.5, 37°C
Aedes aegypti
5.17
-
NADH
recombinant enzyme, pH 7.5, 37°C
Aedes aegypti
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
enzyme is hydrophobis and contains 2 transmembrane segments
Aedes aegypti
16020
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
54000
-
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE
Aedes aegypti
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-kynurenine + NADPH + O2
Aedes aegypti
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
L-kynurenine + NADPH + O2
Aedes aegypti Liverpool
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from soluble fraction of Sf9 insect cells by nickel affinity chromatography
Aedes aegypti
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
L-kynurenine + NADH + H+ + O2
-
658919
Aedes aegypti
3-hydroxy-L-kynurenine + NAD+ + H2O
-
-
-
?
L-kynurenine + NADH + H+ + O2
-
658919
Aedes aegypti Liverpool
3-hydroxy-L-kynurenine + NAD+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
-
658919
Aedes aegypti
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
658919
Aedes aegypti
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
-
658919
Aedes aegypti Liverpool
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
658919
Aedes aegypti Liverpool
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE
Aedes aegypti
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
-
-
Aedes aegypti
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.85
-
NADH
recombinant enzyme, pH 7.5, 37°C
Aedes aegypti
1.88
-
L-kynurenine
recombinant enzyme, pH 7.5, 37°C
Aedes aegypti
2.03
-
NADPH
recombinant enzyme, pH 7.5, 37°C
Aedes aegypti
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Aedes aegypti
Other publictions for EC 1.14.13.9
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)
741802
Tashiro
Kynurenine 3-monooxygenase is ...
Mus musculus
Behav. Brain Res.
317
279-285
2017
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
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-
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-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
742039
Erhardt
Adaptive and behavioral chang ...
Mus musculus
Biol. Psychiatry
82
756-765
2017
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
742081
Phillips
Substrate and inhibitor speci ...
Cytophaga hutchinsonii
Bioorg. Med. Chem. Lett.
27
1705-1708
2017
-
2
-
-
-
-
8
3
-
-
-
1
-
4
-
-
-
-
-
-
-
-
3
-
-
-
-
-
3
-
-
-
-
7
-
-
-
2
-
-
-
-
-
-
8
7
3
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
3
-
-
-
-
-
1
1
-
3
3
742082
Liddle
The discovery of potent and s ...
Homo sapiens
Bioorg. Med. Chem. Lett.
27
2023-2028
2017
-
-
-
-
-
-
31
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
31
-
-
-
1
-
-
-
31
31
-
-
-
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
742478
Gao
Biochemistry and structural s ...
Homo sapiens, Pseudomonas fluorescens
FASEB J.
32
2036-2045
2017
-
1
1
1
25
-
2
-
-
-
2
-
-
5
-
1
1
-
-
-
-
-
2
-
-
2
-
-
-
2
-
-
-
1
-
-
-
1
1
-
1
25
-
-
2
1
-
-
-
2
-
-
-
1
1
-
-
-
-
2
-
2
-
-
-
2
-
-
-
-
1
1
-
-
-
743067
Walker
Development of a series of ky ...
Pseudomonas fluorescens
J. Med. Chem.
60
3383-3404
2017
-
-
-
-
-
-
34
-
-
-
-
-
-
3
-
-
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-
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33
-
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33
34
-
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-
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-
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-
-
-
-
-
1
1
-
-
-
743342
Hutchinson
Structural and mechanistic ba ...
Homo sapiens, Pseudomonas fluorescens
Nat. Commun.
8
15827
2017
-
2
-
-
-
-
12
-
-
-
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-
-
4
-
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-
-
2
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8
-
2
-
2
-
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8
12
-
-
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-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
743358
Gonzalez Esquivel
Kynurenine pathway metabolite ...
Homo sapiens, Rattus norvegicus
Neuropharmacology
112
331-345
2017
-
-
-
-
-
-
-
-
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-
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2
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4
-
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2
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2
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2
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4
-
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2
-
-
-
-
-
-
-
-
-
1
2
2
1
-
-
742349
Smith
Kynurenine-3-monooxygenase a ...
Homo sapiens, Rattus norvegicus, Pseudomonas fluorescens, Sus scrofa
Drug Discov. Today
21
315-324
2016
-
1
-
-
-
-
2
-
2
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7
-
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5
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4
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1
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4
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2
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2
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-
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5
-
-
-
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
743747
Wilson
Bacterial expression of human ...
Homo sapiens
Protein Expr. Purif.
95
96-103
2014
-
-
1
-
-
-
-
4
1
-
-
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-
6
-
-
1
-
-
-
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1
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-
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1
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4
1
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1
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1
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-
-
-
-
-
-
-
-
2
2
-
-
-
724908
Stephens
Kynurenine 3-monooxygenase med ...
Mus musculus
Eur. J. Immunol.
43
1727-1734
2013
-
1
-
-
-
-
-
-
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-
-
-
-
1
-
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1
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1
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1
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1
1
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-
725567
Winkler
Development of LC/MS/MS, high- ...
Homo sapiens
J. Biomol. Screen.
18
879-889
2013
-
1
-
-
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3
1
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7
-
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1
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1
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3
-
1
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3
3
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1
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1
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1
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Kynurenine hydroxylase inhibit ...
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348521
Saito
Kynurenine 3-hydroxylase in br ...
Meriones unguiculatus, Homo sapiens, Macaca mulatta, Mus musculus, Rattus norvegicus
Arch. Biochem. Biophys.
307
104-109
1993
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5
1
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20
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11
5
1
4
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2
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1
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5
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1
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11
5
1
4
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1
2
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1
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348524
Shin
Inhibition of L-kynurenine 3-h ...
Saccharomyces pastorianus
J. Nutr. Sci. Vitaminol.
28
191-201
1982
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4
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3
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4
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4
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1
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348519
McLean-Bowen
Corresponding changes in kynur ...
Saccharomyces cerevisiae
J. Bacteriol.
145
1325-1333
1981
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6
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4
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1
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1
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6
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1
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1
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348523
Stratakis
-
Subcellular localization and p ...
Ephestia kuehniella
J. Comp. Physiol.
141
451-456
1981
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3
2
1
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1
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3
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1
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1
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1
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1
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348518
Nishimoto
Purification of L-kynurenine 3 ...
Rattus norvegicus
J. Chromatogr.
169
357-364
1979
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2
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1
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1
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1
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1
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348516
Nisimoto
Molecular properties of L-kynu ...
Rattus norvegicus
J. Biochem.
81
1413-1425
1977
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1
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1
1
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1
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1
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1
1
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1
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1
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4
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4
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1
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2
1
1
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348517
Nisimoto
Isolation of L-kynurenine 3-hy ...
Rattus norvegicus
J. Biochem.
78
573-581
1975
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1
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1
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348522
Pinamonti
-
Kynurenine-3-hydroxylase of Sc ...
Schistocerca gregaria
Insect Biochem.
4
9-16
1974
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1
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348520
Schott
The regulatory function of L-k ...
Saccharomyces cerevisiae
Hoppe-Seyler's Z. Physiol. Chem.
352
1654-1658
1971
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2
4
1
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1
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2
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4
1
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1
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1
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2
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1
1
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348514
Okamoto
Flavin adenine dinucleotide re ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
29
394-399
1967
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1
3
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3
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1
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3
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2
2
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1
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1
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348515
Saito
Studies on oxygenases: Enzymat ...
Rattus norvegicus, Rattus norvegicus Osborne-Mendel
J. Biol. Chem.
229
921-934
1957
2
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5
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6
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5
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6
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