BRENDA - Enzyme Database
show all sequences of 1.13.11.11

Kynurenine pathway metabolites and enzymes involved in redox reactions

Gonzalez Esquivel, D.; Ramirez-Ortega, D.; Pineda, B.; Castro, N.; Rios, C.; Perez de la Cruz, V.; Neuropharmacology 112, 331-345 (2017)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
H2O2
activation of the enzyme is stimulated by superoxide and H2O2
Homo sapiens
superoxide
activation of the enzyme is stimulated by superoxide and H2O2
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
3-hydroxykynurenine
-
Homo sapiens
Cu2+
-
Homo sapiens
cyanide
-
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.02
-
L-tryptophan
pH and temperature not specified in the publication; pH and temperature not specified in the publication
Homo sapiens
0.19
-
L-tryptophan
pH and temperature not specified in the publication
Homo sapiens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
P14902
-
-
Homo sapiens
P48775
-
-
Homo sapiens
Q6ZQW0
-
-
Mus musculus
P28776
-
-
Xanthomonas campestris pv. campestris
Q8PDA8
-
-
Xanthomonas campestris pv. campestris ATCC 33913
Q8PDA8
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
astrocyte
-
Homo sapiens
-
astrocyte
-
Mus musculus
-
brain
expression on brain occurs in different cells as macrophages, microglia, neurons and astrocytes
Homo sapiens
-
brain
expression on brain occurs in different cells as macrophages, microglia, neurons and astrocytes
Mus musculus
-
kidney
-
Homo sapiens
-
kidney
-
Mus musculus
-
large intestine
-
Homo sapiens
-
large intestine
-
Mus musculus
-
liver
; low level expression; the enzyme is located in the oxygene-rich environment of the liver promoting greater amount of the enzyme in ferric form than in ferrous form, which could contribute to the binding to substrates occurs in this form
Homo sapiens
-
liver
-
Mus musculus
-
lung
-
Homo sapiens
-
lung
-
Mus musculus
-
macrophage
-
Homo sapiens
-
macrophage
-
Mus musculus
-
microglia
-
Homo sapiens
-
microglia
-
Mus musculus
-
additional information
in human tumors IDO-2 is expressed, but it is produced in a functionally inactive form
Homo sapiens
-
neuron
-
Homo sapiens
-
neuron
-
Mus musculus
-
placenta
-
Homo sapiens
-
placenta
-
Mus musculus
-
small intestine
-
Homo sapiens
-
small intestine
-
Mus musculus
-
spleen
-
Homo sapiens
-
spleen
-
Mus musculus
-
stomach
-
Homo sapiens
-
stomach
-
Mus musculus
-
testis
low level expression
Homo sapiens
-
thyroid
low level expression
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tryptophan + O2
-
743358
Homo sapiens
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
the enzyme has broad substrate specificity for various indoleamines such as L-tryptophan and serotonin. It catalyzes the oxidation of the pyrrole ring of tryptophan to form N-formylkynurenine, which is later metabolized to formic acid and kynurenine
743358
Mus musculus
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
the enzyme has broad substrate specificity for various indoleamines such as L-tryptophan and serotonin. It catalyzes the oxidation of the pyrrole ring of tryptophan to form N-formylkynurenine, which is later metabolized to formic acid and kynurenine
743358
Homo sapiens
N-formyl-L-kynurenine
-
-
-
?
Subunits
Subunits
Commentary
Organism
tetramer
-
Xanthomonas campestris pv. campestris
tetramer
-
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
heme
heme-containing enzyme; heme-containing enzyme. The heme prosthetic group is present as a heme-ferric form that must be reduced to the heme-ferrous prior to mediate L-tryptophan oxidation; the enzyme is heme dependent, requiring the reduction of ferric to ferrous-iron to bind to L-tryptophan
Homo sapiens
heme
heme-containing enzyme
Mus musculus
heme
heme-containing enzyme
Xanthomonas campestris pv. campestris
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
H2O2
activation of the enzyme is stimulated by superoxide and H2O2
Homo sapiens
superoxide
activation of the enzyme is stimulated by superoxide and H2O2
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
heme-containing enzyme. The heme prosthetic group is present as a heme-ferric form that must be reduced to the heme-ferrous prior to mediate L-tryptophan oxidation
Homo sapiens
heme
heme-containing enzyme
Homo sapiens
heme
the enzyme is heme dependent, requiring the reduction of ferric to ferrous-iron to bind to L-tryptophan
Homo sapiens
heme
heme-containing enzyme
Mus musculus
heme
heme-containing enzyme
Xanthomonas campestris pv. campestris
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
3-hydroxykynurenine
-
Homo sapiens
Cu2+
-
Homo sapiens
cyanide
-
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.02
-
L-tryptophan
pH and temperature not specified in the publication
Homo sapiens
0.19
-
L-tryptophan
pH and temperature not specified in the publication
Homo sapiens
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
astrocyte
-
Homo sapiens
-
astrocyte
-
Mus musculus
-
brain
expression on brain occurs in different cells as macrophages, microglia, neurons and astrocytes
Homo sapiens
-
brain
expression on brain occurs in different cells as macrophages, microglia, neurons and astrocytes
Mus musculus
-
kidney
-
Homo sapiens
-
kidney
-
Mus musculus
-
large intestine
-
Homo sapiens
-
large intestine
-
Mus musculus
-
liver
the enzyme is located in the oxygene-rich environment of the liver promoting greater amount of the enzyme in ferric form than in ferrous form, which could contribute to the binding to substrates occurs in this form
Homo sapiens
-
liver
-
Homo sapiens
-
liver
low level expression
Homo sapiens
-
liver
-
Mus musculus
-
lung
-
Homo sapiens
-
lung
-
Mus musculus
-
macrophage
-
Homo sapiens
-
macrophage
-
Mus musculus
-
microglia
-
Homo sapiens
-
microglia
-
Mus musculus
-
additional information
in human tumors IDO-2 is expressed, but it is produced in a functionally inactive form
Homo sapiens
-
neuron
-
Homo sapiens
-
neuron
-
Mus musculus
-
placenta
-
Homo sapiens
-
placenta
-
Mus musculus
-
small intestine
-
Homo sapiens
-
small intestine
-
Mus musculus
-
spleen
-
Homo sapiens
-
spleen
-
Mus musculus
-
stomach
-
Homo sapiens
-
stomach
-
Mus musculus
-
testis
low level expression
Homo sapiens
-
thyroid
low level expression
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tryptophan + O2
-
743358
Homo sapiens
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
the enzyme has broad substrate specificity for various indoleamines such as L-tryptophan and serotonin. It catalyzes the oxidation of the pyrrole ring of tryptophan to form N-formylkynurenine, which is later metabolized to formic acid and kynurenine
743358
Mus musculus
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
the enzyme has broad substrate specificity for various indoleamines such as L-tryptophan and serotonin. It catalyzes the oxidation of the pyrrole ring of tryptophan to form N-formylkynurenine, which is later metabolized to formic acid and kynurenine
743358
Homo sapiens
N-formyl-L-kynurenine
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
-
Homo sapiens
tetramer
-
Xanthomonas campestris pv. campestris
Other publictions for EC 1.13.11.11
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)
743153
Nienhaus
Substrate binding primes huma ...
Homo sapiens
J. Phys. Chem. B
121
7412-7420
2017
-
-
-
-
-
-
-
1
-
1
-
1
-
3
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
2
2
-
-
-
743358
Gonzalez Esquivel
Kynurenine pathway metabolite ...
Homo sapiens, Mus musculus, Xanthomonas campestris pv. campestris, Xanthomonas campestris pv. campestris ATCC 33913
Neuropharmacology
112
331-345
2017
2
-
-
-
-
-
3
2
-
-
-
-
-
7
-
-
-
-
-
29
-
-
4
2
-
-
-
-
-
-
-
3
-
-
-
2
-
-
5
-
-
-
-
3
-
3
-
-
-
-
-
-
-
-
-
31
-
-
4
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741938
Basran
Analysis of reaction intermed ...
Homo sapiens, Xanthomonas campestris pv. campestris, Xanthomonas campestris pv. campestris ATCC 33913
Biochemistry
55
6743-6750
2016
-
-
2
-
-
-
-
2
-
2
-
3
-
4
-
-
2
-
-
-
-
-
12
-
2
-
-
-
2
-
-
2
-
-
-
-
-
2
2
-
-
-
-
-
-
2
-
2
-
3
-
-
-
2
-
-
-
-
12
-
2
-
-
-
2
-
-
-
-
4
4
-
-
-
742986
Pantouris
Insights into the mechanism o ...
Homo sapiens
J. Enzyme Inhib. Med. Chem.
31
70-78
2016
-
1
-
-
-
-
2
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
743821
Lewis-Ballester
Molecular basis for catalysis ...
Homo sapiens
Sci. Rep.
6
35169
2016
-
-
1
1
1
-
-
1
-
1
-
1
-
2
-
-
-
1
-
1
-
-
2
1
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
1
1
-
-
-
-
1
-
1
-
1
-
-
-
-
-
1
-
-
2
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
743005
Yuasa
Efficient tryptophan-cataboli ...
Branchiostoma floridae, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Monosiga brevicollis, Nematostella vectensis, no activity in Brugia malayi, no activity in Saccharomyces cerevisiae, no activity in Schistosoma mansoni, Rattus norvegicus, Strongylocentrotus purpuratus
J. Exp. Zool. B
324
128-140
2015
-
-
8
-
-
-
-
11
-
-
-
8
-
14
-
-
-
-
-
-
-
-
8
-
8
-
-
-
3
-
-
1
-
-
-
-
-
8
1
-
-
-
-
-
-
11
-
-
-
8
-
-
-
-
-
-
-
-
8
-
8
-
-
-
3
-
-
-
-
8
8
-
-
-
743064
Wu
Identification of substituted ...
Homo sapiens
J. Med. Chem.
58
7807-7819
2015
-
1
1
-
-
-
21
-
-
-
-
1
-
1
-
-
1
-
-
2
-
-
1
-
1
-
-
-
1
-
-
1
-
-
20
-
1
1
1
-
-
-
20
21
-
-
-
-
-
1
-
-
-
1
-
2
-
-
1
-
1
-
-
-
1
-
-
-
-
3
3
-
-
-
742114
Maeta
Contributions of tryptophan 2 ...
Mus musculus, Mus musculus C57BL/6
Biosci. Biotechnol. Biochem.
78
878-881
2014
-
-
-
-
1
-
-
-
-
-
-
6
-
3
-
-
-
-
-
1
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
6
-
-
-
-
-
1
-
-
8
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
743760
Meng
Structural and functional ana ...
Homo sapiens
Proteins
82
3210-3216
2014
-
-
1
1
9
-
-
8
-
-
-
1
-
2
-
-
1
-
-
1
-
-
3
3
1
-
-
7
1
-
-
1
-
-
-
-
-
1
1
1
9
-
-
-
-
8
-
-
-
1
-
-
-
1
-
1
-
-
3
3
1
-
-
7
1
-
-
-
-
2
2
-
-
-