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Information on EC 1.13.11.52 - indoleamine 2,3-dioxygenase and Organism(s) Mus musculus and UniProt Accession Q8R0V5
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1.13.11.52 indoleamine 2,3-dioxygenaseIUBMB Comments
A protohemoprotein. Requires ascorbic acid and methylene blue for activity. This enzyme has broader substrate specificity than EC 1.13.11.11, tryptophan 2,3-dioxygenase . It is induced in response to pathological conditions and host-defense mechanisms and its distribution in mammals is not confined to the liver . While the enzyme is more active with D-tryptophan than L-tryptophan, its only known function to date is in the metabolism of L-tryptophan [2,6]. Superoxide radicals can replace O2 as oxygen donor [4,7].
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Word Map
- 1.13.11.52
- kynurenine
- dendritic
- t-cells
- lymphocyte
-
immunotherapy
- ifn-gamma
-
immunomodulatory
- autoimmune
- mesenchymal
- interferon-gamma
-
tregs
-
allogeneic
-
immunoregulatory
-
rejection
- serotonin
- heme
- monocyte
-
tolerogenic
-
quinolinic
-
checkpoint
- neopterin
-
allograft
-
immunomodulation
- foxp3
-
antigen-presenting
-
immunoregulation
-
myeloid-derived
- 3-hydroxykynurenine
-
ctla-4
- graft-versus-host
- l-trp
-
3-hydroxyanthranilic
-
quin
-
tumor-infiltrating
-
heme-containing
-
depressive-like
-
immunotherapeutic
-
plasmacytoid
- 5-hydroxytryptamine
-
monocyte-derived
-
ifn-gamma-induced
-
5-hydroxyindoleacetic
-
interferon-gamma-induced
-
immuno-oncology
- drug development
-
cd4+cd25+foxp3+
-
mdscs
- pharmacology
-
alloreactive
-
3-monooxygenase
-
ifn-gamma-mediated
- medicine
-
death-ligand
- synthesis
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
indoleamine 2,3-dioxygenase, indoleamine-2,3-dioxygenase, tryptophan pyrrolase, tryptophan oxygenase, indoleamine 2,3 dioxygenase, indoleamine 2,3-dioxygenase-1, indolamine 2,3-dioxygenase, tryptophan dioxygenase, hido1, indoleamine-pyrrole 2,3-dioxygenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IDO
IDO1
IDO2
indolamine 2,3-dioxygenase
-
-
-
-
indoleamine 2,3-dioxygenase
indoleamine 2,3-dioxygenase-1
indoleamine 2,3-dioxygenase-2
indoleamine 2,3-dioxygenase-like protein
L-tryptophan pyrrolase
-
-
-
-
oxygenase, tryptophan 2,3-di-
-
-
-
-
proto-indoleamine 2,3-dioxygenase
superoxygenase
-
-
-
-
TDO
TO
-
-
-
-
TRPO
-
-
-
-
Tryptamin 2,3-dioxygenase
-
-
-
-
tryptamine 2,3-dioxygenase
-
-
-
-
tryptophan 2,3-dioxygenase
tryptophan oxygenase
-
-
-
-
tryptophan peroxidase
-
-
-
-
tryptophan pyrrolase
-
-
-
-
tryptophanase
-
-
-
-
indoleamine 2,3-dioxygenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
A protohemoprotein. Requires ascorbic acid and methylene blue for activity. This enzyme has broader substrate specificity than EC 1.13.11.11, tryptophan 2,3-dioxygenase [1]. It is induced in response to pathological conditions and host-defense mechanisms and its distribution in mammals is not confined to the liver [2]. While the enzyme is more active with D-tryptophan than L-tryptophan, its only known function to date is in the metabolism of L-tryptophan [2,6]. Superoxide radicals can replace O2 as oxygen donor [4,7].
CAS REGISTRY NUMBER
COMMENTARY
9014-51-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-hydroxy-L-tryptophan + O2
(2S)-4-(2-amino-5-hydroxyphenyl)-2-(formylamino)-4-oxobutanoic acid
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
-
-
-
-
?
L-Trp + O2
L-formylkynurenine
-
enzyme contributes to tumor cell evasion of T cell-mediated rejection
-
-
?
L-Trp + O2
L-formylkynurenine
-
expression of indoleamine 2,3-dioxygenase is an inducible feature of specific subsets of dendritic cells, and provides a potential mechanistic explanation for their T cell regulatory properties
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
-
-
663820, 663910, 665204, 665457, 666461, 666895, 684391, 686721, 687116, 710831, 711165, 712112, 712152, 712821, 713412, 713448, 713586
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
-
IDO represents an important immune regulatory enzyme under diverse physiological and pathological conditions in vivo and is of considerable medical importance
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
-
indoleamine 2,3-dioxygenase is a rate-limiting enzyme in the L-tryptophan-kynurenine pathway. IFN-gamma-induced expression of IDO expression is inhibited only by JAK inhibitor I. Lipopolysaccharide-induced expression of indoleamine 2,3-dioxygenase is inhibited by LY294002 and SP600125 but not by JAK inhibitor I, SB203580, or U0126. LPS can induce the expression of indoleamine 2,3-dioxygenase via an IFN-gamma-independent mechanism and PI3 kinase and JNK in the LPS-induced pathway leading to IDO expression
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
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
-
-
?
additional information
?
-
-
IDO2 enzyme may be involved in immune evasion by tumours
-
-
?
additional information
?
-
IDO2 enzyme may be involved in immune evasion by tumours
-
-
?
additional information
?
-
Trp suppresses 2,3-dioxygenase induction by IFN-gamma at the transcriptional level
-
-
?
additional information
?
-
-
Trp suppresses 2,3-dioxygenase induction by IFN-gamma at the transcriptional level
-
-
?
additional information
?
-
although the kcat of indoleamine-2,3-dioxygenase (IDO) is similar for D-Trp and L-Trp, the Km of IDO is approximately 170fold higher for L-Trp than that for D-Trp
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Trp + O2
L-formylkynurenine
-
enzyme contributes to tumor cell evasion of T cell-mediated rejection
-
-
?
L-Trp + O2
L-formylkynurenine
-
expression of indoleamine 2,3-dioxygenase is an inducible feature of specific subsets of dendritic cells, and provides a potential mechanistic explanation for their T cell regulatory properties
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
-
-
663820, 665204, 666461, 666895, 687116, 710831, 711165, 712112, 712152, 712821, 713412, 713448, 713586
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
-
IDO represents an important immune regulatory enzyme under diverse physiological and pathological conditions in vivo and is of considerable medical importance
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
-
indoleamine 2,3-dioxygenase is a rate-limiting enzyme in the L-tryptophan-kynurenine pathway. IFN-gamma-induced expression of IDO expression is inhibited only by JAK inhibitor I. Lipopolysaccharide-induced expression of indoleamine 2,3-dioxygenase is inhibited by LY294002 and SP600125 but not by JAK inhibitor I, SB203580, or U0126. LPS can induce the expression of indoleamine 2,3-dioxygenase via an IFN-gamma-independent mechanism and PI3 kinase and JNK in the LPS-induced pathway leading to IDO expression
-
-
?
additional information
?
-
-
IDO2 enzyme may be involved in immune evasion by tumours
-
-
?
additional information
?
-
IDO2 enzyme may be involved in immune evasion by tumours
-
-
?
additional information
?
-
Trp suppresses 2,3-dioxygenase induction by IFN-gamma at the transcriptional level
-
-
?
additional information
?
-
-
Trp suppresses 2,3-dioxygenase induction by IFN-gamma at the transcriptional level
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMNH2
-
4-5-fold higher activity than acitivity with methylene blue as the electron donor
heme
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-hydroxy-D-tryptophan
-
0.1 mM, 26% inhibition of cleavage of D-tryptophan, 29% inhibition of cleavage of L-tryptophan
5-hydroxy-L-tryptophan
-
0.1 mM, 40% inhibition of cleavage of D-tryptophan, 53% inhibition of cleavage of L-tryptophan
dexamethasone
-
inhibits IDO activity in brain and lung after systemic pokeweed mitogen administration and brains of mice suffering from malaria
indole-3-acetic acid
-
1 mM, 19% inhibition of cleavage of D-tryptophan, 27% inhibition of cleavage of L-tryptophan
iodoacetic acid
-
1 mM, 12% inhibition of cleavage of D-tryptophan, 7% inhibition of cleavage of L-tryptophan
KCN
-
0.01 mM, 39% inhibition of cleavage of D-tryptophan, 48% inhibition of cleavage of L-tryptophan
N-(3-((1H-benzo[d]imidazol-1-yl)methyl)benzyl)-1H-indole-2-carboxamide
-
-
N-(3-((1H-benzo[d]imidazol-1-yl)methyl)benzyl)-4-bromo-1H-pyrrole-2-carboxamide
selective inhibitor of IDO1 against L-Trp dioxygenase (TDO) at 0.001 mM, yet when the concentration is increased up to 0.010 mM, an inhibition of TDO is observed to some extent
-
N-ethylmaleimide
-
1 mM, 58% inhibition of cleavage of D-tryptophan, 45% inhibition of cleavage of L-tryptophan
NaN3
-
10 mM, 33% inhibition of cleavage of D-tryptophan, 32% inhibition of cleavage of L-tryptophan
serotonin
-
1 mM, 36% inhibition of cleavage of D-tryptophan, 37% inhibition of cleavage of L-tryptophan
tenatoprazole
-
highly selective for IDO2 inhibition, no inhibition of IDO1 or tryptophan dioxygenase
Tiron
-
10 mM, 2% inhibition of cleavage of D-tryptophan, 6% inhibition of cleavage of L-tryptophan
tryptamine
-
0.1 mM, 16% inhibition of cleavage of D-tryptophan, 11% inhibition of cleavage of L-tryptophan
1-methyl-D-tryptophan
-
poor non-competitive inhibitor of both IDO1 and IDO2 activity
1-methyl-D-tryptophan
-
the isomer is more effective in inhibiting IDO than 1-methyl-L-tryptophan
1-methyl-DL-tryptophan
-
pharmacologic inhibition of indoleamine 2,3-dioxygenase skews cytokine responses of invariant natural killer T cells towards a Th1 profile
1-methyl-L-tryptophan
-
the isomer is less effective in inhibiting IDO than 1-methyl-D-tryptophan
1-methyl-L-tryptophan
-
better inhibitor of IDO2 enzymatic activity than 1DMT in both cell-free and cellular assays
1-Methyltryptophan
-
treatment of pregnant mice result in rapid T-cell-induces rejection of allogeneic concepti
additional information
-
inhibition of indoleamine 2,3-dioxygenase may be developed as an anticancer immunotherapeutic strategy
-
additional information
-
review article sumarizing data of many inhibitors of indoleamine 2,3-dioxygenase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.028
L-tryptophan
-
recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C
0.028
L-tryptophan
-
IDO1, pH and temperature not specified in the publication, MB assay
0.029
L-tryptophan
-
recombinant isozyme IDO1, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C
0.029
L-tryptophan
-
IDO1, pH and temperature not specified in the publication, cytochrome b5 assay
0.53
L-tryptophan
-
recombinant isozyme IDO2, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C
0.53
L-tryptophan
-
IDO1, pH and temperature not specified in the publication, cytochrome b5 assay
12
L-tryptophan
-
recombinant isozyme IDO2, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C
12
L-tryptophan
-
IDO1, pH and temperature not specified in the publication, MB assay
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.3
1-methyl-D-tryptophan
-
recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C
1.6
L-tryptophan
-
inhibition of IDO1, pH and temperature not specified in the publication
0.0018
tenatoprazole
-
IDO2, pH and temperature not specified in the publication
additional information
additional information
-
review article sumarizing data of many inhibitors of indoleamine 2,3-dioxygenase
-
0.08
1-methyl-L-tryptophan
-
recombinant isozyme IDO1, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C
0.105
1-methyl-L-tryptophan
-
recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C
0.44
1-methyl-L-tryptophan
-
recombinant isozyme IDO2, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C
2.75
1-methyl-L-tryptophan
-
recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C
0.69
norharman
-
recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C
1.08
norharman
-
recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C
1.73
norharman
-
recombinant isozyme IDO1, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C
1.96
norharman
-
recombinant isozyme IDO2, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000093 - 0.0000132
N-(3-((1H-benzo[d]imidazol-1-yl)methyl)benzyl)-1H-indole-2-carboxamide
-
0.00000546 - 0.0000127
N-(3-((1H-benzo[d]imidazol-1-yl)methyl)benzyl)-4-bromo-1H-pyrrole-2-carboxamide
-
additional information
additional information
Mus musculus
-
review article sumarizing data of many inhibitors of indoleamine 2,3-dioxygenase
-
0.0000093
N-(3-((1H-benzo[d]imidazol-1-yl)methyl)benzyl)-1H-indole-2-carboxamide
Mus musculus
pH and temperature not specified in the publication, in cell line P1.IDO1
-
0.0000132
N-(3-((1H-benzo[d]imidazol-1-yl)methyl)benzyl)-1H-indole-2-carboxamide
Mus musculus
pH and temperature not specified in the publication, in cell line P1.TDO
-
0.00000546
N-(3-((1H-benzo[d]imidazol-1-yl)methyl)benzyl)-4-bromo-1H-pyrrole-2-carboxamide
Mus musculus
pH and temperature not specified in the publication, in cell line P1.TDO
-
0.0000127
N-(3-((1H-benzo[d]imidazol-1-yl)methyl)benzyl)-4-bromo-1H-pyrrole-2-carboxamide
Mus musculus
pH and temperature not specified in the publication, in cell line P1.IDO1
-
0.0000323
N-(3-((1H-benzo[d]imidazol-1-yl)methyl)benzyl)-4-cyanobenzamide
Mus musculus
pH and temperature not specified in the publication, in cell line P1.TDO
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.55
-
25°C, 50 mM HEPES/NaOH (pH 7.3), 5 mM D-tryptophan 0.01 mM methylene blue, 5 mM ascorbic acid, 0.001 mM catalase
2.13
-
25°C, 50 mM HEPES/NaOH (pH 7.3), 2 mM L-tryptophan 0.01 mM methylene blue, 5 mM ascorbic acid, 0.001 mM catalase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 6.5
7.4 - 7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
-
pH 5.0: about 50% of maximal activity, pH 7.0: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
consistently expresses the enzyme at low levels. Exposure to UV-light leads to a dose-responding upregulation. Overexpression of indoleamine-pyrrole 2,3-dioxygenase could reduce apoptosis significantly following UV-B irradiation
-
IDO-competent cells exhibit attributes of B cells as well as dendritic cells
-
IDO-competent cells are present in spleens of B-cell-deficient mice
additional information
-
enzyme activity in triple transgenic Alzheimer's disease mice. Expression of TDO mRNA is significantly increased in the cerebellum of Alzheimer's disease mouse brain
expression on brain occurs in different cells as macrophages, microglia, neurons and astrocytes
-
the expression of the enzyme is selectively induced in specific splenic dendritic cell subsets when mice are exposed to the synthetic immunomodulatory reagent CTLA4-Ig
-
neurons, level of activity is lower than in monocytic cells in lymph nodes
-
the enzyme is upregulated by interferon-gamma in neurons of the hippocampus
-
IDO is highly expressed throughout the intestine with a marked presence in the jejunum and ileum both at the RNA and protein level
-
IDO is highly expressed throughout the intestine with a marked presence in the jejunum and ileum both at the RNA and protein level
-
IDO is highly expressed throughout the intestine with a marked presence in the jejunum and ileum both at the RNA and protein level
-
tubular epithelial cell. Expression of indoleamine 2,3-dioxygenase may be deleterious during renal inflammation, because it enhances TEC self-injury through Fas/FasL interactions. Attenuation of indoleamine 2,3-dioxygenase may represent a novel strategy to promote kidney function following ischemia and renal allograft rejection
-
the enzyme is upregulated by interferon-gamma in neurons of the hippocampus. The enzyme could contribute to the vulnerability of neurons to inflammatory conditions
additional information
-
IDO is not detected in CD103- gut dendritic cells and in spleen
additional information
-
IDO1 expression is found in most tissues and is regulated by immunological signals, including interferon-gamma, lipopolysaccharide and tumor necrosis factor. Expression of IDO2 protein in the liver and kidney in these IDO1-/- mice is unaffected, although the IDO2 transcript is downregulated. It is possible that the deletion of the IDO1 gene affects the expression of the IDO2 protein in other cell types, and 1DMT's effects might be mediated through either or both IDO isoforms
additional information
-
quantitative real-time RT PCR enzyme expression analysis in brain sectiions
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview. Some lineages have independently generated multiple IDO paralogues through gene duplications. Only mammalian IDO1s and fungal typical IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Phylogenetic analysis. the phylogenetic distribution of low catalytic-efficiency IDOs indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. IDOs with high catalytic-efficiency for L-Trp catabolism may have evolved in certain lineages to fulfill particular biological roles. The low catalytic efficiency IDOs have been well conserved in a number of lineages throughout their evolution, although it is not clear that the enzymes contribute significantly to L-Trp catabolism in these species
evolution
indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview. Some lineages have independently generated multiple IDO paralogues through gene duplications. Only mammalian IDO1s and fungal typical IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Phylogenetic analysis. the phylogenetic distribution of low catalytic-efficiency IDOs indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. IDOs with high catalytic-efficiency for L-Trp catabolism may have evolved in certain lineages to fulfill particular biological roles. The low catalytic efficiency IDOs have been well conserved in a number of lineages throughout their evolution, although it is not clear that the enzymes contribute significantly to L-Trp catabolism in these species
malfunction
metabolism
physiological function
additional information
-
transcription of the IDO2 gene is complex. IDO1 expression is found in most tissues and is regulated by immunological signals, including interferon-gamma, lipopolysaccharide and tumor necrosis factor
malfunction
-
IDO deficiency leads to diminished phenotypic and functional maturation of dendritic cells in vitro and in vivo
malfunction
-
IDO inhibition significantly affects the ability of CD103+ dendritic cells to promote conversion of naive T cells into Foxp3+Tregs while the ability of CD103- cells is unaffected. IDO inhibition impinges on the development of oral tolerance
malfunction
-
the attenuation of Francisella novicida tryptophan mutant bacteria is rescued in the lungs of IDO1-deficient mice
malfunction
-
IDO1 pharmacological inhibition causes the rejection of mouse allogeneic concepti, mediated by T cells, and its expression in tumors is associated with their immune evasion. Deletion of IDO1 genomic sequences has the potential to also impact on IDO2 expression due to the chromosomal proximity of the genes, transcription of the IDO2 gene is reduced in the liver of IDO1-/- mice, although protein levels appear to be maintained
malfunction
-
the kynurenine pathway is over-activated in Alzheimer's disease mice
metabolism
-
IDO is a key enzyme that catalyzes the initial, rate-limiting step in tryptophan degradation
metabolism
-
three enzymes are now known to catalyze the first and rate-limiting step in the catabolism of tryptophan along the kynurenine pathway: tryptophan 2,3-dioxygenase, indoleamine 2,3-dioxygenase subsequently and a third enzyme, indoleamine 2,3-dioxygenase 2. The kynurenine pathway is a major route for NAD+ synthesis. The pathway is implicated in many disorders and/or their complications, including cerebral malaria, neurological and neurodegenerative diseases
metabolism
-
tryptophan 2,3 dioxygenase is the key regulatory enzyme of the kynurenine pathway
metabolism
comparison of contribution percentage of tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) and indoleamine 2,3-dioxygenase (IDO) to the conversion of L-tryptophan, the calculated percentage conversions indicats that TDO and IDO oxidize 70% and 30%, respectively, of the dietary L-tryptophan. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low, this amount of D-Trp is converted to L-Trp, which is primarily used for protein synthesis rather than catabolism via the Kyn biosynthesis pathway in mice
physiological function
-
activation of IDO is a key event in the switch from sickness to depression, activation of the innate immune system in the brain is sufficient to activate IDO and to induce depressive-like behavior in the absence of detectable interferon-gamma
physiological function
-
IDO is a mechanism for Kupffer cells to induce immune tolerance
physiological function
-
indoleamine 2,3-dioxygenase 1 is a lung-specific innate immune defense mechanism that inhibits growth of Francisella tularensis tryptophan auxotrophs
physiological function
-
indoleamine 2,3-dioxygenase is an enzyme involved in tryptophan catabolism with immunosuppressive effects influencing T regulatory/T effector cell balance and oral tolerance induction
physiological function
-
TDO expression distinguishes stem cells from more differentiated cells among the granule cells of the adult mouse dentate gyrus. TDO is required at a late-stage of granule cell development, such as during axonal and dendritic growth, synaptogenesis and its maturation
physiological function
-
immune regulatory effects of Ido1 and ability of nitric oxide to regulate Ido1 activity, Ido1-mediated metabolism of tryptophan to kynurenine can modulate vascular tone After transient cerebral ischaemia induction in wild-type and Ido1 gene-deficient (Ido1-/-) mice, cerebral ischaemia-reperfusion in wild-type mice increases Ido activity and its expression in cerebral arterioles, while Ido1-/- and 1-methyl-D-tryptophan-treated wild-type mice have lower Ido activity but similar post-stroke neurological function and similar total brain infarct volume and swelling, relative to control mice. Ido1 expression does not appear to affect overall outcome following acute ischaemic stroke
physiological function
-
in mammals, IDO1 acts as a defence molecule in combating bacterial and viral infections, as its expression is up-regulated by cytokines such as IFN-gamma, leading to local depletion of L-Trp and causing inhibition of pathogen growth. IDO2 mRNA is also upregulated in the brain of mice infected with Toxoplasma gondii, an infection in which IFN-gamma driven responses play an important role in controlling parasite growth
physiological function
the enzyme is involved in nicotinamide biosynthesis. Comparison of contribution percentage of tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) and indoleamine 2,3-dioxygenase (IDO) to the conversion of L-tryptophan, the calculated percentage conversions indicats that TDO and IDO oxidize 70% and 30%, respectively, of the dietary L-tryptophan. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low, this amount of D-Trp is converted to L-Trp, which is primarily used for protein synthesis rather than catabolism via the Kyn biosynthesis pathway in mice
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
tetramer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48 - 60
-
the melting temperature of the denaturation process for recombinant isozyme IDO1 is 60°C, with a possible second intermediate at 48°C, recombinant isozyme IDO2 denatures in a single step, with a melting temperature at 48°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, hydroxyapatite column chromatography (two times), gel filtration, DEAE cellulose column chromatography, third hydroxyapatite column chromatography, Sephadex G-200 gel filtration, second DEAE cellulose column chromatography
-
homogenization, ammonium sulfate precipitation, gel filtration with Sephacryl S200, Bio-gel HT column, stored at -75°C
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Ido2, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX. No complementation of the enzyme-deficient Saccharomyces cerevisiae
cell-free transcription/translation using a wheat germ system, expression in COS-7 cell
-
gene IDO1, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX. No complementation of the enzyme-deficient Saccharomyces cerevisiae
isozyme IDO2 is expressed in KRX cells, isozyme IDO1 is expressed in Escherichia coli Rosetta cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
IDO expression in bone marrow-derived dendritic cells is increased by hemin, a potent inducer of heme oxygenase-1
-
IDO expression is abrogated by the heme oxygenase inhibitor zinc protoporphrin (5 mg/kg, i.p.). Heme oxygenase-1 downregulation decreases lipopolysaccharide-induced IDO expression in murine dendritic cells. Lipopolysaccharide induces high IDO expression
-
IDO1 expression is upregulated by cytokines such as IFN-gamma, IDO2 is upregulated in mouse dendritic cell lines as well as mouse mesenchymal stem cells. IDO2 mRNA is also upregulated in the brain of mice infected with Toxoplasma gondii, an infection in which IFN-gamma-driven responses play an important role in controlling parasite growth
-
in mice heterozygous for the alpha-isoform of calcium/calmodulin-dependent protein kinase II, in which dentate gyrus granule cells fail to mature normally, TDO immunoreactivity is substantially downregulated in the dentate gyrus granule cells
-
isozyme IDO 1 (but not isozyme IDO2) is induced specifically in the lungs of mice infected with Francisella novicida or Streptococcus pneumonia
-
TDO expression gradually increases with the development of granule cells. new neurons begin to express TDO between 2 and 4 weeks after the neurons are generated, when the axons and dendrites of the granule cells develop and synaptogenesis occurs
-
the expression of TDO mRNA is significantly increased in the cerebellum of Alzheimer's disease mouse brain
-
transient stimulation of the innate immune system by an intraperitoneal injection of lipopolysaccharide (100 ng) activates peripheral and central expression of indoleamine 2,3 dioxygenase. Addition of lipopolysaccharide (10 ng/ml) to the medium of organotypic hippocampal slice cultures induces steady-state expression of mRNA transcripts for IDO that peaks at 6 h and translates into increased IDO enzymatic activity within 8 h post-lipopolysaccharide
-
treatment of Pax5iGFP/iGFP knockin mice with CpG oligonucleotides (CpG B 1826 with a fully phosphorothioate backbone, 0.1 mg, i.v.) induces IDO expression
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
expression of indoleamine 2,3-dioxygenase may be deleterious during renal inflammation, because it enhances TEC self-injury through Fas/FasL interactions. Attenuation of indoleamine 2,3-dioxygenase may represent a novel strategy to promote kidney function following ischemia and renal allograft rejection
medicine
-
indoleamine 2,3-dioxygenase activity might be of therapeutic utility in allergen immunotherapy. Indoleamine 2,3-dioxygenase-dependent tryptophan metabolites contribute to tolerance induction during allergen immunotherapy in a mouse model
medicine
-
target for therapeutic intervention. Inhibition of inappropriate IDO activity in tumours in vivo may attenuate the ability of tumours to evade immune surveillance and promote clearance. Strategies that enhance IDO activity during autoimmune or inflammatory diseases may be beneficial via inhibition of undesirable T cell activities
medicine
-
systemic IDO activity, determined as the kynurenine/tryptophan ratio in serum, correlates with the presence of palpable tumor. IDO mediates immune suppression in the early stages of prostate cancer progression. IDO expression in the tumor tissue is irrelevant for transgenic adenocarcinoma of mouse prostate tumor incidence
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Central role of tryptophan pyrrolase in haem metabolism
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575-583
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Bos taurus, Cavia porcellus, Gallus gallus, Oryctolagus cuniculus, Felis catus, Frog, Meriones unguiculatus, Cricetinae, Ovis aries, Homo sapiens, Meleagris gallopavo, Mus musculus, Rattus norvegicus, Sus scrofa
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Indoleamine 2,3-dioxygenase contributes to tumor cell evasion of T cell-mediated rejection
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101
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Mus musculus
Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
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Mus musculus (P48776)
Habara-Ohkubo, A.; Takikawa, O.; Yoshida, R.
Cloning and expression of a cDNA encoding mouse indoleamine 2,3-dioxygenase
Gene
105
221-227
1991
Mus musculus (P28776), Mus musculus
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Cutting edge: induced indoleamine 2,3-dioxygenase expression in dendritic cell subsets suppresses T cell clonal expansion
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171
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2003
Mus musculus
Ozaki, Y.; Reinhard, J.F., Jr.; Nichol, C.A.
Cofactor activity of dihydroflavin mononucleotide and tetrahydrobiopterin for murine epididymal indoleamine 2,3-dioxygenase
Biochem. Biophys. Res. Commun.
137
1106-1111
1986
Mus musculus
Watanabe, Y.; Fujiwara, M.; Yoshida, R.; Hayaishi, O.
Stereospecificity of hepatic L-tryptophan 2,3-dioxygenase
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189
393-405
1980
Bos taurus, Capra hircus, Oryctolagus cuniculus, Homo sapiens, Macaca fuscata fuscata, Mus musculus, Pseudomonas fluorescens, Rattus norvegicus, Sus scrofa
Fallarino, F.; Vacca, C.; Orabona, C.; Belladonna, M.L.; Bianchi, R.; Marshall, B.; Keskin, D.B.; Mellor, A.L.; Fioretti, M.C.; Grohmann, U.; Puccetti, P.
Functional expression of indoleamine 2,3-dioxygenase by murine CD8 alpha(+) dendritic cells
Int. Immunol.
14
65-68
2002
Mus musculus, Mus musculus DBA/2J
Takikawa, O.; Yoshida, R.; Kido, R.; Hayaishi, O.
Tryptophan degraadation in mice initiated by indoleamine 2,3-dioxygenase
J. Biol. Chem.
261
3648-3653
1986
Mus musculus
Roy, E.J.; Takikawa, O.; Kranz, D.M.; Brown, A.R.; Thomas, D.L.
Neuronal localization of indoleamine 2,3-dioxygenase in mice
Neurosci. Lett.
387
95-99
2005
Mus musculus
Thomas, S.R.; Stocker, R.
Redox reactions related to indoleamine 2,3-dioxygenase and tryptophan metabolism along the kynurenine pathway
Redox Rep.
4
199-220
1999
Oryctolagus cuniculus, Homo sapiens, Mus musculus
Serbecic, N.; Beutelspacher, S.C.
Indoleamine 2,3-dioxygenase protects corneal endothelial cells from UV mediated damage
Exp. Eye Res.
82
416-426
2006
Mus musculus (P28776), Mus musculus
Mohib, K.; Guan, Q.; Diao, H.; Du, C.; Jevnikar, A.M.
Proapoptotic activity of indoleamine 2,3-dioxygenase expressed in renal tubular epithelial cells
Am. J. Physiol. Renal Physiol.
293
F801-F812
2007
Mus musculus
Austin, C.J.; Astelbauer, F.; Kosim-Satyaputra, P.; Ball, H.J.; Willows, R.D.; Jamie, J.F.; Hunt, N.H.
Mouse and human indoleamine 2,3-dioxygenase display some distinct biochemical and structural properties
Amino Acids
36
99-106
2009
Mus musculus, Homo sapiens (P14902), Homo sapiens
Okamoto, T.; Tone, S.; Kanouchi, H.; Miyawaki, C.; Ono, S.; Minatogawa, Y.
Transcriptional regulation of indoleamine 2,3-dioxygenase (IDO) by tryptophan and its analogue
Cytotechnology
54
107-113
2007
Mus musculus (P28776), Mus musculus
Jung, I.D.; Lee, C.M.; Jeong, Y.I.; Lee, J.S.; Park, W.S.; Han, J.; Park, Y.M.
Differential regulation of indoleamine 2,3-dioxygenase by lipopolysaccharide and interferon gamma in murine bone marrow derived dendritic cells
FEBS Lett.
581
1449-1456
2007
Mus musculus
Ball, H.J.; Sanchez-Perez, A.; Weiser, S.; Austin, C.J.; Astelbauer, F.; Miu, J.; McQuillan, J.A.; Stocker, R.; Jermiin, L.S.; Hunt, N.H.
Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice
Gene
396
203-213
2007
Homo sapiens (Q6ZQW0), Homo sapiens, Mus musculus (Q8R0V5), Mus musculus
Molano, A.; Illarionov, P.A.; Besra, G.S.; Putterman, C.; Porcelli, S.A.
Modulation of invariant natural killer T cell cytokine responses by indoleamine 2,3-dioxygenase
Immunol. Lett.
117
81-90
2008
Mus musculus
King, N.J.; Thomas, S.R.
Molecules in focus: indoleamine 2,3-dioxygenase
Int. J. Biochem. Cell Biol.
39
2167-2172
2007
Homo sapiens, Mus musculus
Ball, H.J.; Yuasa, H.J.; Austin, C.J.; Weiser, S.; Hunt, N.H.
Indoleamine 2,3-dioxygenase-2; a new enzyme in the kynurenine pathway
Int. J. Biochem. Cell Biol.
41
467-471
2009
Mus musculus, Mus musculus (B1AC39)
Taher, Y.A.; Piavaux, B.J.; Gras, R.; van Esch, B.C.; Hofman, G.A.; Bloksma, N.; Henricks, P.A.; van Oosterhout, A.J.
Indoleamine 2,3-dioxygenase-dependent tryptophan metabolites contribute to tolerance induction during allergen immunotherapy in a mouse model
J. Allergy Clin. Immunol.
121
983-91.e2
2008
Mus musculus
Yuasa, H.J.; Takubo, M.; Takahashi, A.; Hasegawa, T.; Noma, H.; Suzuki, T.
Evolution of vertebrate indoleamine 2,3-dioxygenases
J. Mol. Evol.
65
705-714
2007
Homo sapiens (P14902), Mus musculus (P28776), Mus musculus, Rattus norvegicus (Q9ERD9)
Macchiarulo, A.; Camaioni, E.; Nuti, R.; Pellicciari, R.
Highlights at the gate of tryptophan catabolism: a review on the mechanisms of activation and regulation of indoleamine 2,3-dioxygenase (IDO), a novel target in cancer disease
Amino Acids
37
219-229
2009
Mus musculus, Homo sapiens (P14902)
Rafice, S.A.; Chauhan, N.; Efimov, I.; Basran, J.; Raven, E.L.
Oxidation of L-tryptophan in biology: a comparison between tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase
Biochem. Soc. Trans.
37
408-412
2009
Saccharomyces cerevisiae, Oryctolagus cuniculus, Drosophila melanogaster, Homo sapiens, Mus musculus, Cupriavidus metallidurans, Xanthomonas campestris
Yuasa, H.J.; Ball, H.J.; Ho, Y.F.; Austin, C.J.; Whittington, C.M.; Belov, K.; Maghzal, G.J.; Jermiin, L.S.; Hunt, N.H.
Characterization and evolution of vertebrate indoleamine 2, 3-dioxygenases IDOs from monotremes and marsupials
Comp. Biochem. Physiol. B
153
137-144
2009
Danio rerio, Mus musculus, Xenopus laevis, Ornithorhynchus anatinus (B3Y9H6), Ornithorhynchus anatinus (B3Y9H7), Monodelphis domestica (B3Y9H8), Monodelphis domestica (B3Y9H9), Monodelphis domestica
Cherayil, B.J.
Indoleamine 2,3-dioxygenase in intestinal immunity and inflammation
Inflamm. Bowel Dis.
15
1391-1396
2009
Homo sapiens, Mus musculus
Dai, X.; Zhu, B.T.
Indoleamine 2,3-Dioxygenase Tissue Distribution and Cellular Localization in Mice: Implications for Its Biological Functions
J. Histochem. Cytochem.
58
17-28
2009
Mus musculus (P28776), Mus musculus
Kanai, M.; Funakoshi, H.; Takahashi, H.; Hayakawa, T.; Mizuno, S.; Matsumoto, K.; Nakamura, T.
Tryptophan 2,3-dioxygenase is a key modulator of physiological neurogenesis and anxiety-related behavior in mice
Mol. Brain
2
8
2009
Mus musculus
Kanai, M.; Nakamura, T.; Funakoshi, H.
Identification and characterization of novel variants of the tryptophan 2,3-dioxygenase gene: differential regulation in the mouse nervous system during development
Neurosci. Res.
64
111-117
2009
Mus musculus
Xu, H.; Oriss, T.B.; Fei, M.; Henry, A.C.; Melgert, B.N.; Chen, L.; Mellor, A.L.; Munn, D.H.; Irvin, C.G.; Ray, P.; Ray, A.
Indoleamine 2,3-dioxygenase in lung dendritic cells promotes Th2 responses and allergic inflammation
Proc. Natl. Acad. Sci. USA
105
6690-6695
2008
Mus musculus
Austin, C.J.; Mailu, B.M.; Maghzal, G.J.; Sanchez-Perez, A.; Rahlfs, S.; Zocher, K.; Yuasa, H.J.; Arthur, J.W.; Becker, K.; Stocker, R.; Hunt, N.H.; Ball, H.J.
Biochemical characteristics and inhibitor selectivity of mouse indoleamine 2,3-dioxygenase-2
Amino Acids
39
565-578
2010
Mus musculus
Jung, I.D.; Lee, J.S.; Lee, C.M.; Noh, K.T.; Jeong, Y.I.; Park, W.S.; Chun, S.H.; Jeong, S.K.; Park, J.W.; Son, K.H.; Heo, D.R.; Lee, M.G.; Shin, Y.K.; Kim, H.W.; Yun, C.H.; Park, Y.M.
Induction of indoleamine 2,3-dioxygenase expression via heme oxygenase-1-dependant pathway during murine dendritic cell maturation
Biochem. Pharmacol.
80
491-505
2010
Mus musculus
Matteoli, G.; Mazzini, E.; Iliev, I.D.; Mileti, E.; Fallarino, F.; Puccetti, P.; Chieppa, M.; Rescigno, M.
Gut CD103+ dendritic cells express indoleamine 2,3-dioxygenase which influences T regulatory/T effector cell balance and oral tolerance induction
Gut
59
595-604
2010
Homo sapiens, Mus musculus
Peng, K.; Monack, D.M.
Indoleamine 2,3-dioxygenase 1 is a lung-specific innate immune defense mechanism that inhibits growth of Francisella tularensis tryptophan auxotrophs
Infect. Immun.
78
2723-2733
2010
Mus musculus
Fu, X.; Zunich, S.M.; OConnor, J.C.; Kavelaars, A.; Dantzer, R.; Kelley, K.W.
Central administration of lipopolysaccharide induces depressive-like behavior in vivo and activates brain indoleamine 2,3 dioxygenase in murine organotypic hippocampal slice cultures
J. Neuroinflammation
7
43
2010
Mus musculus
Ohira, K.; Hagihara, H.; Toyama, K.; Takao, K.; Kanai, M.; Funakoshi, H.; Nakamura, T.; Miyakawa, T.
Expression of tryptophan 2,3-dioxygenase in mature granule cells of the adult mouse dentate gyrus
Mol. Brain
3
26
2010
Mus musculus
Johnson, B.A.; Kahler, D.J.; Baban, B.; Chandler, P.R.; Kang, B.; Shimoda, M.; Koni, P.A.; Pihkala, J.; Vilagos, B.; Busslinger, M.; Munn, D.H.; Mellor, A.L.
B-lymphoid cells with attributes of dendritic cells regulate T cells via indoleamine 2,3-dioxygenase
Proc. Natl. Acad. Sci. USA
107
10644-10648
2010
Mus musculus
Kaellberg, E.; Wikstroem, P.; Bergh, A.; Ivars, F.; Leanderson, T.
Indoleamine 2,3-dioxygenase (IDO) activity influence tumor growth in the TRAMP prostate cancer model
Prostate
70
1461-1470
2010
Mus musculus
Yan, M.L.; Wang, Y.D.; Tian, Y.F.; Lai, Z.D.; Yan, L.N.
Inhibition of allogeneic T-cell response by Kupffer cells expressing indoleamine 2,3-dioxygenase
World J. Gastroenterol.
16
636-640
2010
Mus musculus
Fatokun, A.A.; Hunt, N.H.; Ball, H.J.
Indoleamine 2,3-dioxygenase 2 (IDO2) and the kynurenine pathway: characteristics and potential roles in health and disease
Amino Acids
45
1319-1329
2013
Homo sapiens, Mus musculus
Jackman, K.A.; Brait, V.H.; Wang, Y.; Maghzal, G.J.; Ball, H.J.; McKenzie, G.; De Silva, T.M.; Stocker, R.; Sobey, C.G.
Vascular expression, activity and function of indoleamine 2,3-dioxygenase-1 following cerebral ischaemia-reperfusion in mice
Naunyn Schmiedebergs Arch. Pharmacol.
383
471-481
2011
Mus musculus
Wu, W.; Nicolazzo, J.A.; Wen, L.; Chung, R.; Stankovic, R.; Bao, S.S.; Lim, C.K.; Brew, B.J.; Cullen, K.M.; Guillemin, G.J.
Expression of tryptophan 2,3-dioxygenase and production of kynurenine pathway metabolites in triple transgenic mice and human Alzheimers disease brain
PLoS ONE
8
e59749
2013
Homo sapiens, Mus musculus
Maeta, A.; Sano, M.; Fukuwatari, T.; Funakoshi, H.; Nakamura, T.; Shibata, K.
Contributions of tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase to the conversion of D-tryptophan to nicotinamide analyzed by using tryptophan 2,3-dioxygenase-knockout mice
Biosci. Biotechnol. Biochem.
78
878-881
2014
Mus musculus (P28776), Mus musculus C57BL/6 (P28776)
Yuasa, H.J.; Ball, H.J.
Efficient tryptophan-catabolizing activity is consistently conserved through evolution of TDO enzymes, but not IDO enzymes
J. Exp. Zool. B
324
128-140
2015
Strongylocentrotus purpuratus, Xenopus laevis (A2BD60), Nematostella vectensis (A7SDW8), Monosiga brevicollis (A9UVU0), Danio rerio (B0V1K8), Branchiostoma floridae (C3Y9Y8), Homo sapiens (P14902), Mus musculus (P28776), Mus musculus (Q8R0V5), Haliotis diversicolor (Q6F3I3)
Gonzalez Esquivel, D.; Ramirez-Ortega, D.; Pineda, B.; Castro, N.; Rios, C.; Perez de la Cruz, V.
Kynurenine pathway metabolites and enzymes involved in redox reactions
Neuropharmacology
112
331-345
2017
Homo sapiens (P14902), Homo sapiens (Q6ZQW0), Mus musculus (P28776)
Serafini, M.; Torre, E.; Aprile, S.; Grosso, E.D.; Gesu, A.; Griglio, A.; Colombo, G.; Travelli, C.; Paiella, S.; Adamo, A.; Orecchini, E.; Coletti, A.; Pallotta, M.T.; Ugel, S.; Massarotti, A.; Pirali, T.; Fallarini, S.
Discovery of highly potent benzimidazole derivatives as indoleamine 2,3-dioxygenase-1 (IDO1) inhibitors from structure-based virtual screening to in vivo pharmacodynamic activity
J. Med. Chem.
63
3047-3065
2020
Mus musculus (P28776)
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