Information on EC 1.13.11.52 - indoleamine 2,3-dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
1.13.11.52
-
RECOMMENDED NAME
GeneOntology No.
indoleamine 2,3-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-tryptophan + O2 = N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
L-tryptophan + O2 = N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
L-tryptophan + O2 = N-formyl-L-kynurenine
show the reaction diagram
density functional theory calculations have been performed to elucidate the reaction mechanism of oxidative cleavage of Trp
-
L-tryptophan + O2 = N-formyl-L-kynurenine
show the reaction diagram
Criegee type rearrangement for ring opening
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-tryptophan degradation I (via anthranilate)
-
-
L-tryptophan degradation to 2-amino-3-carboxymuconate semialdehyde
-
-
L-tryptophan degradation XI (mammalian, via kynurenine)
-
-
Metabolic pathways
-
-
Tryptophan metabolism
-
-
tryptophan metabolism
-
-
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].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IDO
P28776
-
IDO
Mus musculus DBA/2J
-
-
-
IDO
Q9ERD9
-
IDO-2
-
-
IDO1
P14902
-
IDO1
-
isozyme
IDO2
F5H5G0
-
IDO2
-
isozyme
INDOL1
-
-
INDOL1
Q6ZQW0
-
INDOL1
Q8R0V5
-
indole 2,3-dioxygenase
-
-
indoleamine 2, 3-dioxygenase
-
-
indoleamine 2,3 dioxygenase
-
-
indoleamine 2,3 dioxygenase
-
-
indoleamine 2,3-dioxygenase
P14902
-
indoleamine 2,3-dioxygenase
-
-
indoleamine 2,3-dioxygenase
P28776
-
indoleamine 2,3-dioxygenase 1
-
-
indoleamine 2,3-dioxygenase 1
P14902
-
indoleamine 2,3-dioxygenase 1
-
-
indoleamine 2,3-dioxygenase 2
-
-
indoleamine 2,3-dioxygenase 2
F5H5G0
-
indoleamine 2,3-dioxygenase 2
-
-
indoleamine 2,3-dioxygenase-1
-
-
indoleamine 2,3-dioxygenase-2
-
-
indoleamine 2,3-dioxygenase-2
-
-
indoleamine 2,3-dioxygenase-like protein
-
-
indoleamine 2,3-dioxygenase-like protein
Q6ZQW0
-
indoleamine 2,3-dioxygenase-like protein
-
-
indoleamine 2,3-dioxygenase-like protein
Q8R0V5
-
indoleamine-2,3-dioxygenase
-
-
Indoleamine-pyrrole 2,3-dioxygenase
P28776
-
mIDO
-
-
proto-IDO
-
-
proto-indoleamine 2,3-dioxygenase
-
-
tryptophan dioxygenase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9014-51-1
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
IDO1
SwissProt
Manually annotated by BRENDA team
IDO2
UniProt
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
with lung cancer
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
; C57BL6J and murine cell lines P815B murine mastocytoma cells
-
-
Manually annotated by BRENDA team
DBA/2J
-
-
Manually annotated by BRENDA team
male specific-pathogen-free ICR mice
-
-
Manually annotated by BRENDA team
pregnant
-
-
Manually annotated by BRENDA team
Mus musculus DBA/2J
DBA/2J
-
-
Manually annotated by BRENDA team
male Sprague-Dawley
-
-
Manually annotated by BRENDA team
Sprague Dawley
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
IDO inhibition significantly affects the ability of CD103+ denxritic 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
-
hemodialysis patients characterized by impaired adaptive immunity, exhibit increased IDO expression, further enhanced in the non-responders to hepatitis B virus vaccination
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
metabolism
-
IDO catalyzes the initial and rate-limiting step in the catabolism of tryptophan along the kynurenine pathway
metabolism
-
IDO is a key enzyme that catalyzes the initial, rate-limiting step in tryptophan degradation
metabolism
-
IDO is the first and rate-limiting enzyme in the kynurenine pathway
metabolism
-
indoleamine 2,3-dioxygenase catalyses the initial rate-limiting step of tryptophan degradation along the kynurenine pathway
metabolism
-
indoleamine 2,3-dioxygenase catalyzes the first step in tryptophan breakdown along the kynurenine pathway
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 inhibits lymphocyte proliferation induced by lectins
physiological function
-
IDO is a mechanism for Kupffer cells to induce immune tolerance
physiological function
-
IDO is an immunoregulatory enzyme that is implicated in suppressing T-cell immunity in normal and pathological settings. IDO5-specific T cells are specifically able to kill IDO-expressing cells. IDO-specific T cells boost viral immunity
physiological function
-
IDO is central in the regulation of immune responses
physiological function
-
IDO is involved in the maintenance of immune tolerance at the maternal-fetal interface
physiological function
-
IDO-1 is one of the key players involved in the pathogenesis of Alzheimer's disease
physiological function
-
IDO-expressing skin substitutes significantly suppress T cell infiltration and improve neovascularization by 4fold
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 activity is implicated in the promotion of tolerance to tumors and in autoimmune and inflammatory conditions, itplays a role in arthritis, ischemia-reperfusion injury, haemostatic system, sepsis, atherosclerosis, diabetes, and gut, allergy, and airway inflammation
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
-
indoleamine 2,3-dioxygenase is critical for regulating immune responses and suppression of inflammation. In human chronic granulomatous disease, IDO metabolic activity is intact
physiological function
-
indoleamine 2,3-dioxygenase mediates the antiviral effect of interferon-gamma against hepatitis B virus in human hepatocyte-derived cells, indoleamine 2,3-dioxygenase efficiently reduces the level of intracellular hepatitis B virus DNA without altering the steady-state level of viral RNA
physiological function
-
the induction of IDO by interferon-gamma in HLE-B3 cells causes increases in intracellular reactive oxygen species, cytosolic cytochrome c and caspase-3 activity, along with a decrease in protein-free thiol content, are accompanied by apoptosis. IDO-mediated kynurenine formation plays a role in cataract formation related to chronic inflammation
physiological function
-
heme enzyme indoleamine 2,3-dioxygenase is a key regulator of immune responses through catalyzing L-tryptophan oxidation. Peroxidase-mediated dioxygenase inactivation, NO consumption, or protein nitration may modulate the biological actions of IDO expressed in inflammatory tissues where the levels of H2O2 and NO are elevated and L-Trp is low
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
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
-
indoleamine 2,3-dioxygenase suppresses adaptive immunity. It induces T-cell differentiation to regulatory T-cells through tryptophan depletion and/or kynurenine pathway products. The enzyme decreases glucose uptake by stimulated lymphocytes, increases mitochondrial function in stimulated lymphocytes, decreases aerobic glycolysis in stimulated lymphocytes, and induces the production of the immunosuppressive cytokine IL-10 by stimulated lymphocytes. Effect of IDO on glucose metabolism of lymphocytes, overview
physiological function
-
the enzyme is responsible for L-Trp processing that ultimately leads to the biosynthesis of NAD+ and NADP+
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
additional information
-
H2O2 activates the peroxidase function to induce protein oxidation and inhibit dioxygenase activity, overview. Dioxygenase inhibition correlated with IDO-catalyzed H2O2 consumption, compound I-mediated formation of protein-centered radicals, altered protein secondary structure, and opening of the distal heme pocket to promote nonproductive substrate binding, inhibited by L-Trp, the heme ligand cyanide, or free radical scavengers
additional information
-
IDO1 and IDO2 have different kinetic parameters and different inhibition profiles
additional information
-
molecular dynamics simulation studies, overview. Structural role of T342 in controlling the substrate stereoselectivity of the enzyme
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-benzofuran-DL-tryptophan + O2
?
show the reaction diagram
-
1 mM, 22% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
1-benzothiophene-DL-tryptophan + O2
?
show the reaction diagram
-
1 mM, 19% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
1-methyl-DL-tryptophan + O2
?
show the reaction diagram
-
1 mM, 7% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
1-methyl-L-tryptophan + O2
?
show the reaction diagram
-
-
-
-
?
2-bromo-L-tryptophan + O2
?
show the reaction diagram
-
1 mM, 21% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
2-chloro-L-tryptophan + O2
?
show the reaction diagram
-
1 mM, 33% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
2-hydroxy-L-tryptophan + O2
?
show the reaction diagram
-
1 mM, 4% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
3-indoleethanol + O2-
?
show the reaction diagram
-
-
-
-
?
3-N-aminoethyl-tryptophan + O2
?
show the reaction diagram
-
1 mM, 32% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
4-methyl-DL-tryptophan + O2
?
show the reaction diagram
-
1 mM, 33% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
5-benzyloxy-DL-tryptophan + O2
?
show the reaction diagram
-
1 mM, 1% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
5-bromo-DL-tryptophan + O2
?
show the reaction diagram
-
1 mM, 36% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
5-fluoro-DL-tryptophan + O2
?
show the reaction diagram
-
1 mM, 46% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
5-fluoro-tryptophan + O2
4-(2-amino-5-fluorophenyl)-2-(formylamino)-4-oxobutanoic acid
show the reaction diagram
-
-
-
-
?
5-fluorotryptophan + O2
?
show the reaction diagram
-
-
-
-
?
5-hydroxy-L-tryptophan + O2
?
show the reaction diagram
-
-
-
-
?
5-hydroxy-L-tryptophan + O2
?
show the reaction diagram
-
1 mM, 59% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
5-hydroxy-L-tryptophan + O2
N-formyl-5-hydroxy-L-kynurenine
show the reaction diagram
-
-
-
-
?
5-hydroxy-L-tryptophan + O2
N-formyl-5-hydroxy-L-kynurenine
show the reaction diagram
-
-
-
-
?
5-hydroxy-L-tryptophan + O2
N-formyl-5-hydroxy-L-kynurenine
show the reaction diagram
-
-
-
-
?
5-hydroxy-L-tryptophan + O2
(2S)-4-(2-amino-5-hydroxyphenyl)-2-(formylamino)-4-oxobutanoic acid
show the reaction diagram
-
-
-
-
?
5-hydroxy-tryptophan + O2
4-(2-amino-5-hydroxyphenyl)-2-(formylamino)-4-oxobutanoic acid
show the reaction diagram
-
-
-
-
?
5-hydroxytryptamine + O2
?
show the reaction diagram
-
-
-
-
?
5-hydroxytryptophan + O2
?
show the reaction diagram
-
-
-
-
?
5-hydroxytryptophan + O2-
N-formyl-5-hydroxykynurenine
show the reaction diagram
-
-
-
-
?
5-methoxy-D,L-tryptophan + O2
?
show the reaction diagram
-
1 mM, 70% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
5-methyl-D,L-tryptophan + O2
?
show the reaction diagram
-
1 mM, 123% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
5-methyl-tryptophan + O2
4-(2-amino-5-methylphenyl)-2-(formylamino)-4-oxobutanoic acid
show the reaction diagram
-
-
-
-
?
5-methyltryptophan + O2
?
show the reaction diagram
-
-
-
-
?
6-fluoro-DL-tryptophan + O2
?
show the reaction diagram
-
1 mM, 38% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
6-fluorotryptophan + O2
?
show the reaction diagram
-
-
-
-
?
6-methyl-DL-tryptophan + O2
?
show the reaction diagram
-
1 mM, 72% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
6-nitro-L-tryptophan + O2
?
show the reaction diagram
-
1 mM, 2% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
7-methyl-DL-tryptophan + O2
?
show the reaction diagram
-
1 mM, 18% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
alpha-methyl-DL-tryptophan + O2
?
show the reaction diagram
-
1 mM, 35% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
alpha-methyl-DL-tryptophan + O2-
?
show the reaction diagram
-
-
-
-
?
alpha-N-methyl-L-tryptophan + O2
?
show the reaction diagram
-
1 mM, 21% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
beta-methyl-DL-tryptophan + O2
?
show the reaction diagram
-
1 mM, 32% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
D-Trp + O2
D-formylkynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
?
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
F5H5G0, P14902
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
Q9ERD9
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
low activity
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
IDO displays a similar kcat for D- and L-tryptophan, but D-tryptophan has 173folds higher Km
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
L-Trp is a better substrate for IDO than D-Trp
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
IDO1
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
IDO1
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
Mus musculus DBA/2J
-
-
-
-
?
D-tryptophan + O2
D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2-
N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2-
N-formyl-D-kynurenine
show the reaction diagram
-
O2- binds first to the ferric enzyme and is followed by rapid binding of L-tryptophan
-
-
?
indole + O2-
?
show the reaction diagram
-
-
-
-
?
kynurenine
?
show the reaction diagram
-
-
-
-
?
L-Trp + O2
L-formylkynurenine
show the reaction diagram
-
-
-
-
?
L-Trp + O2
L-formylkynurenine
show the reaction diagram
-
-
-
-
?
L-Trp + O2
L-formylkynurenine
show the reaction diagram
-
proposed reaction mechanism involves the proton abstraction by iron-bound dixoygen. The O-O bond is precisely controlled by the heme proximal and distal environment and is not cleaved before the incorporation of both oxygen atoms into the substrate
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
P14902
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
P28776
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
-
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
F5H5G0, P14902
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
Q9ERD9
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
higher affinity at alkaline pH than at acidic pH
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
no activity with oxygen concentrations below 0.1 mM, maximum activity at 1.15 mM oxygen
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
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
show the reaction diagram
-
plays an important role in the immune response by catalyzing the oxidative degradation of L-tryptophan that contributes to immune suppression and tolerance
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
IDO displays a similar kcat for D- and L-tryptophan, but D-tryptophan has 173folds higher Km
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
L-Trp is a better substrate for IDO than D-Trp
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
human TDO displays a major specificity towards L-Trp, structural role of T342 in controlling the substrate stereoselectivity of the enzyme
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
IDO1 and IDO2
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
IDO1 and IDO2
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
highly preferred substrate, T342 plays a pivotal role in controlling the substrate stereoselectivity of hTDO
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
Mus musculus DBA/2J
-
-
-
-
?
L-tryptophan + O2
L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formylkynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formylkynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2-
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2-
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2-
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan ethyl ester + O2
?
show the reaction diagram
-
1 mM, 14% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
N-acetyl-L-tryptophan + O2
?
show the reaction diagram
-
1 mM, 3% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
serotonin + O2
?
show the reaction diagram
-
-
-
-
?
serotonin + O2
?
show the reaction diagram
-
-
-
-
?
serotonin + O2-
?
show the reaction diagram
-
-
-
-
?
Trp + O2
formylkynurenine
show the reaction diagram
-
-
-
-
?
tryptamine + O2
?
show the reaction diagram
-
-
-
-
?
tryptamine + O2
?
show the reaction diagram
-
-
-
-
?
tryptamine + O2-
?
show the reaction diagram
-
-
-
-
?
tryptophan + O2
N-formylkynurenine
show the reaction diagram
-
if the cellular environment protects indoleamine 2,3-dioxygenase from oxidation to the ferric form, no additional electron donor might by required for indolamine 2,3-dioxygenase activity in intact tissues
-
-
?
L-tryptophan methyl ester + O2
?
show the reaction diagram
-
1 mM, 15% activity relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
-
?
additional information
?
-
-
not active with indoleacetic acid and skatole
-
-
-
additional information
?
-
-
the enzyme plays an important physiological role in the defense mechanism against a variety of infectious pathogens, in the regulation of T-cell function by macrophages and a subset of dendritic cells, and in the synthesis of UV filters in human lenses. Serious problems arise from the unregulated over-expression of the enzyme, which often results in a deleterious systemic Trp depletion and/or the accumulation of neurotoxin, quinolinic acidn the brain. Enzyme expression in malignant tumors helps them to avoid the immune surveillance through a local Trp depletion. The kynurenilation of the lens protein with UV filters thus appears to be the major cause of age-related cataract
-
-
-
additional information
?
-
-
IDO2 enzyme may be involved in immune evasion by tumours
-
-
-
additional information
?
-
-
the IDO enzyme is involved in the immune regulation of early atherosclerosis, particularly in young female adults
-
-
-
additional information
?
-
-
Trp suppresses 2,3-dioxygenase induction by IFN-gamma at the transcriptional level
-
-
-
additional information
?
-
-
docking calculations and spatial coarse graining simulations are used to determine the molecular basis of substrate recognition, enhancer binding and conformational transitions of IDO in response to these events
-
-
-
additional information
?
-
-
the enzyme acts as a heme peroxidase that, in the absence of substrates, self-inactivates dioxygenase activity via compound I-initiated protein oxidation. L-Trp protects against dioxygenase inactivation by reacting with compound I and retarding compound II reduction to suppress peroxidase turnover. Catalytic cycle of hemeperoxidase enzymes, and enzyme peroxidase mechanism, overview
-
-
-
additional information
?
-
-
the enzyme catalyzes the oxidation of indole by H2O2, with generation of 2- and 3-oxoindole as the major products, in the absence of O2 and reducing agents and is not inhibited by superoxide dismutase or hydroxyl radical scavengers, although it is strongly inhibited by L-Trp. IDO inserts oxygen into indole in a reaction that is mechanistically analogous to the peroxide shunt pathway of cytochrome P450
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-hydroxy-L-tryptophan + O2
N-formyl-5-hydroxy-L-kynurenine
show the reaction diagram
-
-
-
-
?
5-hydroxy-L-tryptophan + O2
N-formyl-5-hydroxy-L-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
F5H5G0, P14902
-
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
IDO displays a similar kcat for D- and L-tryptophan, but D-tryptophan has 173folds higher Km
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
L-Trp is a better substrate for IDO than D-Trp
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
IDO1
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
-
IDO1
-
-
?
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
Mus musculus DBA/2J
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
F5H5G0, P14902
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
higher affinity at alkaline pH than at acidic pH
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
no activity with oxygen concentrations below 0.1 mM, maximum activity at 1.15 mM oxygen
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
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
show the reaction diagram
-
plays an important role in the immune response by catalyzing the oxidative degradation of L-tryptophan that contributes to immune suppression and tolerance
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
IDO displays a similar kcat for D- and L-tryptophan, but D-tryptophan has 173folds higher Km
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
L-Trp is a better substrate for IDO than D-Trp
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
human TDO displays a major specificity towards L-Trp, structural role of T342 in controlling the substrate stereoselectivity of the enzyme
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
IDO1 and IDO2
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
IDO1 and IDO2
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
Mus musculus DBA/2J
-
-
-
-
?
serotonin + O2
?
show the reaction diagram
-
-
-
-
?
serotonin + O2
?
show the reaction diagram
-
-
-
-
?
tryptamine + O2
?
show the reaction diagram
-
-
-
-
?
tryptamine + O2
?
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2-
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme plays an important physiological role in the defense mechanism against a variety of infectious pathogens, in the regulation of T-cell function by macrophages and a subset of dendritic cells, and in the synthesis of UV filters in human lenses. Serious problems arise from the unregulated over-expression of the enzyme, which often results in a deleterious systemic Trp depletion and/or the accumulation of neurotoxin, quinolinic acidn the brain. Enzyme expression in malignant tumors helps them to avoid the immune surveillance through a local Trp depletion. The kynurenilation of the lens protein with UV filters thus appears to be the major cause of age-related cataract
-
-
-
additional information
?
-
-
IDO2 enzyme may be involved in immune evasion by tumours
-
-
-
additional information
?
-
-
the IDO enzyme is involved in the immune regulation of early atherosclerosis, particularly in young female adults
-
-
-
additional information
?
-
-
Trp suppresses 2,3-dioxygenase induction by IFN-gamma at the transcriptional level
-
-
-
additional information
?
-
-
the enzyme acts as a heme peroxidase that, in the absence of substrates, self-inactivates dioxygenase activity via compound I-initiated protein oxidation. L-Trp protects against dioxygenase inactivation by reacting with compound I and retarding compound II reduction to suppress peroxidase turnover. Catalytic cycle of hemeperoxidase enzymes, and enzyme peroxidase mechanism, overview
-
-
-
additional information
?
-
-
the enzyme catalyzes the oxidation of indole by H2O2, with generation of 2- and 3-oxoindole as the major products, in the absence of O2 and reducing agents and is not inhibited by superoxide dismutase or hydroxyl radical scavengers, although it is strongly inhibited by L-Trp. IDO inserts oxygen into indole in a reaction that is mechanistically analogous to the peroxide shunt pathway of cytochrome P450
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMNH2
-
4-5-fold higher activity than acitivity with methylene blue as the electron donor
heme
-
none of the polar amino acid residues in the distal heme pocket are essential for activity. The O-O bond is precisely controlled by the heme proximal and distal environment and is not cleaved before the incorporation of both oxygen atoms into the substrate
heme
-
recombinant isozymes IDO2 and IDO1 are ferric (Fe3+) type heme proteins
heme
-
IDO is active when the heme iron is in the ferrous (Fe2+) form and inactive when it is in ferric (Fe3+) form
heme
-
the active-site heme is essential for IDO dioxygenase activity, reduction of heme from the ferric (FeIII) to the ferrous (FeII) form facilitates binding of O2 and L-Trp to form the active ternary complex
tetrahydrobiopterin
-
-
methylene blue
-
stimulates the formation of D-kynurenine
additional information
-
ascorbic acid in combination with methylene blue or toluidine blue; superoxide anion in combination with methylene blue or toluidine blue
-
additional information
-
ascorbic acid, can be replaced by xanthine oxidase with hypoxanthine; not affected by hydrogen peroxide; toluidine blue, can replace methylene blue
-
additional information
-
O2-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CN-
-
enhances the affinity for L-tryptophan for the ferric enzyme in reziprocal manner, positive cooperativity
F-
-
enhances the affinity for L-tryptophan for the ferric enzyme in reziprocal manner, positive cooperativity
Fe2+
-
heme-containing enzyme
Fe2+
-
heme-containing enzyme, reduction of heme from the ferric (FeIII) to the ferrous (FeII) form facilitates binding of O2 and L-Trp to form the active ternary complex
Fe2+
-
heme-containing enzyme
N3-
-
enhances the affinity for L-tryptophan for the ferric enzyme in reziprocal manner, positive cooperativity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2,4-dichlorophenyl)methanethiol
-
-
(2-chlorophenyl)methanethiol
-
-
(3,4-dichlorophenyl)methanethiol
-
-
(3-hydroxyphenyl)(phenyl)methanone
-
-
(3R,4S and 3S,4R)-3-bromo-4-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3R,4S and 3S,4R)-3-hydroxy-2,2-dimethyl-4-morpholino-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3R,4S and 3S,4R)-3-hydroxy-4-methoxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3R,4S and 3S,4R)-4-(allylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3R,4S and 3S,4R)-4-(benzylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3R,4S and 3S,4R)-4-(benzylthio)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3R,4S and 3S,4R)-4-(butylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3S,4S and 3R,4R)-3,4-dihydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
alpha-lapachone
(3S,4S and 3R,4R)-3-hydroxy-2,2-dimethyl-4-morpholino-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3S,4S and 3R,4R)-3-hydroxy-4-methoxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3S,4S and 3R,4R)-4-(allylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3S,4S and 3R,4R)-4-(benzylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3S,4S and 3R,4R)-4-(benzyloxy)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3S,4S and 3R,4R)-4-(benzylthio)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3S,4S)-4-(benzylamino)-3,9-dihydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(3S,4S)-4-(butylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
(4-chlorophenyl)methanethiol
-
-
(4-chlorophenyl)methanol
-
-
(4-fluorophenyl)methanethiol
-
-
(4-methoxyphenyl)methanethiol
-
-
(4-methylphenyl)methanethiol
-
-
(4E,4'E)-4,4'-bis(isopropylimino)-2,2'-binaphthyl-1,1'-(4H,4'H)-dione
-
-
-
(4E,4'E)-4,4'-bis(pentan-3-ylimino)-2,2'-binaphthyl-1,1'-(4H,4'H)-dione
-
-
-
(E)-4-(isopropylimino)-2-methylnaphthalen-1(4H)-one
-
-
-
(R)-2-amino-N-(4-hydroxynaphth-1-yl)propanamide
-
-
-
(S)-2-amino-5-((R)-1-(carboxymethylamino)-3-(1,4-dihydroxy-3-methylnaphthalen-2-ylthio)-1-oxopropan-2-ylamino)-5-oxopentanoic acid
-
-
(S)-2-amino-5-((R)-1-(carboxymethylamino)-3-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-ylthio)-1-oxopropan-2-ylamino)-5-oxopentanoic acid
-
-
(S)-2-amino-N-(4-hydroxynaphth-1-yl)propanamide
-
-
-
1,2-naphthoquinone
-
-
1,4-naphtho-quinone
-
-
1-(1,3-benzothiazol-2-ylsulfanyl)-N,N-dimethylmethanamine
-
-
1-(4-chlorobenzyl)urea
-
-
1-(4-chlorophenyl)methanamine
-
-
1-(4-chlorophenyl)thiourea
-
-
1-benzofuran-DL-tryptophan
-
1 mM, 43% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
1-benzothiophene-DL-tryptophan
-
1 mM, 16% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
1-benzyl-5-phenyl-1H-imidazole
-
-
1-methyl-D-tryptophan
-
IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan
1-methyl-D-tryptophan
-
IDO inhibitor with selectivity for IDO2
1-methyl-D-tryptophan
-
-
1-methyl-D-tryptophan
-
poor non-competitive inhibitor of both IDO1 and IDO2 activity
1-methyl-D-tryptophan
-
competitive inhibitor
1-methyl-D-tryptophan
-
the isomer is more effective in inhibiting IDO than 1-methyl-L-tryptophan
1-methyl-D-tryptophan
-
selective inhibition of IDO2, 1DMT is not efficacious in a tumor model on an IDO1-/- background
1-methyl-D-tryptophan
-
-
1-methyl-DL-tryptophan
-
competitive inhibition with L-tryptophan, 2 mM, 70% inhibition
1-methyl-DL-tryptophan
-
competitive inhibitor
1-methyl-DL-tryptophan
-
1 mM, 26% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
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-DL-tryptophan
-
-
1-methyl-DL-tryptophan
-
-
1-methyl-L-tryptophan
-
-
1-methyl-L-tryptophan
-
substrate inhibition, 1-methyl-D-tryptophan exhibits no inhibitory effect
1-methyl-L-tryptophan
-
poor competitive inhibitor of isozyme IDO1
1-methyl-L-tryptophan
-
competitive inhibitor
1-methyl-L-tryptophan
-
the isomer is less effective in inhibiting IDO than 1-methyl-D-tryptophan
1-methyl-L-tryptophan
-
-
1-methyl-L-tryptophan
-
better inhibitor of IDO2 enzymatic activity than 1DMT in both cell-free and cellular assays
1-methyl-tryptophan
-
-
1-methyl-tryptophan
-
-
1-methyl-tryptophan
-
competitive
1-Methyltryptophan
-
treatment of pregnant mice result in rapid T-cell-induces rejection of allogeneic concepti
1-[2-(4-chlorophenyl)ethyl]thiourea
-
-
1H-benzotriazole
-
-
2,2-dimethyl-1a,9b-dihydro-2H-benzo[g]oxireno[c]chromene-4,9-dione
-
-
2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
dehydro-alpha-lapachone
2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
2,2-dimethyl-3,4-epoxy-2H-naphtho[2,3-b]pyran-5,10-dione
-
-
2,3-dichloro-1,4-naphthoquinone
-
-
2,4-dichlorobenzyl carbamimidothioate hydrobromide
-
-
2-(1H-imidazol-4-yl)benzene-1,3-diol
-
-
2-(1H-imidazol-4-yl)benzenethiol
-
-
2-(1H-imidazol-4-yl)phenol
-
-
2-(1H-pyrazol-3-yl)phenol
-
-
2-(2-chlorophenyl)ethyl carbamimidothioate hydrobromide
-
-
2-(3-chlorophenyl)ethyl carbamimidothioate hydrobromide
-
-
2-(4-chlorophenyl)ethanamine
-
-
2-(4-chlorophenyl)ethyl carbamimidothioate hydrobromide
-
-
2-([5-(3-methoxyphenyl)[1,3]thiazolo[2,3-c][1,2,4]triazol-3-yl]sulfanyl)-N-(5-methyl-1,3-thiazol-2-yl)acetamide
F5H5G0, P14902
poor inhibitor; poor inhibitor
2-amino-3-hydroxy-N-(4-hydroxynaphthalen-1-yl)propanamide
-
-
2-amino-N-(4-hydroxynaphth-1-yl)acetamide
-
-
-
2-bromo-L-tryptophan
-
1 mM, 11% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
2-chloro-L-tryptophan
-
1 mM, 20% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
2-chlorobenzyl carbamimidothioate hydrochloride
-
-
2-Hydroxy-1,4-naphthoquinone
-
-
2-hydroxy-L-tryptophan
-
1 mM, 30% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
2-hydroxygarveatin E
-
-
2-hydroxygarvin A
-
-
2-mercaptobenzothiazole
-
-
2-methoxy-1,4-naphthoquinone
-
-
2-methyl-1,4-naphthoquinone
-
-
2-methylnaphthalene-1,4-dione
-
-
2-phenoxyaniline
-
-
-
3,4-dichlorobenzyl carbamimidothioate hydrochloride
-
-
3-(1H-1,2,3-triazol-5-yl)pyridine
-
-
3-(1H-imidazol-4-yl)benzaldehyde
-
-
3-(1H-imidazol-4-yl)benzenethiol
-
-
3-(1H-imidazol-4-yl)benzonitrile
-
-
3-(1H-imidazol-4-yl)phenol
-
-
3-(4H-imidazol-4-yl)benzenethiol
-
-
3-chlorobenzyl carbamimidothioate hydrochloride
-
-
3-hydroxy-2,2-dimethyl-4-(morpholin-4-yl)-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
3-hydroxy-4-methoxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
3-indoleethanol
-
lowers Km value for D-tryptophan by 25% at pH 7, enhances Vmax by 40-60%
3-N-aminoethyl-tryptophan
-
1 mM, 28% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
-
3-phenylpyridine
-
-
4-(1H-1,2,3-triazol-5-yl)pyridine
-
-
4-(1H-imidazol-4-yl)phenol
-
-
4-(2,6-dimethoxyphenyl)-1H-imidazole
-
-
4-(2-(diethylamino)ethylamino)-1-naphthol
-
-
-
4-(2-(methylthio)phenyl)-1H-imidazole
-
-
4-(2-fluorophenyl)-1H-imidazole
-
-
4-(2-hydroxyethoxy)-1-naphthol
-
-
-
4-(3-(methylthio)phenyl)-1H-imidazole
-
-
4-(3-fluorophenyl)-1H-imidazole
-
-
4-(4-(methylthio)phenyl)-1H-imidazole
-
-
4-(4-fluorophenyl)-1H-imidazole
-
-
4-(benzylamino)-1-naphthol
-
-
-
4-(benzylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
4-(butylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
4-(cyclohexylamino)-1-naphthol
-
-
-
4-(dimethylamino)naphthalen-1-ol
-
-
4-(ethylamino)-1-naphthol
-
-
-
4-(isobutylamino)-1-naphthol
-
-
-
4-(isopropylamino)-1-naphthol
-
-
-
4-(methylamino)naphthalen-1-ol
-
-
4-(pent-3-ylamino)-1-naphthol
-
-
-
4-(phenylcarbonyl)benzyl carbamimidothioate hydrobromide
-
-
4-(propan-2-yl)benzyl carbamimidothioate hydrobromide
-
-
4-(propylamino)-1-naphthol
-
-
-
4-(tert-butylamino)naphthalen-1-ol
-
-
4-(thiophen-2-yl)-1H-imidazole
-
-
4-(trifluoromethyl)benzyl carbamimidothioate hydrochloride
-
-
4-amino-1,2,3-oxadiazole-3-carboximidamide
-
-
-
4-amino-1,2,5-oxadiazole-3-carboximidamide
-
competitive
4-amino-1-naphthol
-
-
4-amino-N'-hydroxy-N-(3-isopropylphenyl)-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N'-hydroxy-N-(3-methoxyphenyl)-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N'-hydroxy-N-(3-methylphenyl)-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N'-hydroxy-N-phenyl-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N-(2-chlorophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N-(3-bromo-4-fluorophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N-(3-bromophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N-(3-chloro-4-fluorophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N-(3-chlorophenyl)-1,2,5-oxadiazole-3-carbohydrazonamide
-
-
4-amino-N-(3-chlorophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N-(3-ethylphenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N-(3-fluorophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N-(3-tert-butylphenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N-(4-chlorophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
4-amino-N-benzyl-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
4-bromo-5-(4-methylphenyl)-1H-1,2,3-triazole
-
-
4-bromobenzyl carbamimidothioate hydrobromide
-
-
4-chlorobenzenesulfonic acid
-
-
4-chlorobenzenethiol
-
-
4-chlorobenzyl carbamimidothioate hydrochloride
-
-
4-chlorobenzyl N,N'-dimethylcarbamimidothioate - 1-chlorotetraoxidane (1:1)
-
-
4-cyanobenzyl carbamimidothioate hydrobromide
-
-
4-ethylbenzyl carbamimidothioate hydrochloride
-
-
4-fluoro-2-(1H-pyrazol-3-yl)phenol
-
-
4-fluorobenzyl carbamimidothioate hydrochloride
-
-
4-hydroxycarbazole
-
-
-
4-iodo-5-phenyl-1H-1,2,3-triazole
-
-
4-methoxy-1-naphthylamine
-
-
4-methoxybenzyl carbamimidothioate hydrochloride
-
-
4-methyl-DL-tryptophan
-
1 mM, 26% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
4-methylbenzyl carbamimidothioate hydrochloride
-
-
4-nitro-5-(4-nitrophenyl)-1H-1,2,3-triazole
-
-
4-nitrobenzyl carbamimidothioate hydrochloride
-
-
4-phenyl-1,3-thiazol-2-amine
-
-
4-phenyl-1,3-thiazole-2-thiol
-
-
4-phenylimidazole
-
heme ligand, non competitive, 0.1 M potassium phosphate buffer (pH 5.5-8), 0.1 M Tris-HCl buffer (pH 7.5-8), 25C
4-phenylimidazole
-
-
4-phenylimidazole
-
weak noncompetitive inhibitor of IDO
4-tert-butylbenzyl carbamimidothioate hydrobromide
-
-
4-[(carbamimidoylsulfanyl)methyl]benzoic acid hydrochloride
-
-
4-[2-(methylsulfanyl)phenyl]-1H-imidazole
-
-
4-[3-(methylsulfanyl)phenyl]-1H-imidazole
-
-
5-(2-bromophenyl)-1H-1,2,3-triazole
-
-
5-(2-chlorophenyl)-1H-1,2,3-triazole
-
-
5-(2-methoxyphenyl)-1H-1,2,3-triazole
-
-
5-(4-bromophenyl)-1H-1,2,3-triazole
-
-
5-(4-chlorophenyl)-1H-1,2,3-triazole
-
-
5-(4-fluorophenyl)-1H-1,2,3-triazole
-
-
5-(4-methoxyphenyl)-1H-1,2,3-triazole
-
-
5-(ethylamino)quinolin-8-ol
-
-
-
5-(isopropylamino)quinolin-8-ol
-
-
-
5-amino-8-hydroxyquinoline
-
-
-
5-benzyloxy-DL-tryptophan
-
1 mM, 2% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
5-bromo-DL-tryptophan
-
1 mM, 56% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
5-chloro-1,3-benzothiazole-2(3H)-thione
-
-
5-fluoro-DL-tryptophan
-
1 mM, 32% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
5-hydroxy-1,4-naphthoquinone
-
-
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
5-hydroxy-L-tryptophan
-
1 mM, 12% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
5-methoxy-DL-tryptophan
-
1 mM, 35% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
5-methyl-DL-tryptophan
-
1 mM, 6% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
5-phenyl-1H-1,2,3-triazole
-
-
6-fluoro-DL-tryptophan
-
1 mM, 54% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
6-hydroxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
6-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
6-methoxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
6-methyl-DL-tryptophan
-
1 mM, 20% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
6-nitro-D-tryptophan
-
1 mM, 7% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
6-nitro-L-tryptophan
-
1 mM, competitive inhibition, 52% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
7-hydroxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
7-methoxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
7-methyl-DL-tryptophan
-
1 mM, 36% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
8-hydroxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
8-methoxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
9-fluorenone
-
-
9-hydroxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
alpha-caryopterone
9-hydroxyfluorene
-
-
9-methoxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
alpha-methyl-DL-tryptophan
-
1 mM, 1% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
alpha-N-methyl-L-tryptophan
-
1 mM, 33% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
annulin A
-
-
baicalein
-
uncompetitive reversible potent IDO-1 inhibitor
benzophenone
-
-
benzyl carbamimidothioate hydrochloride
-
-
Berberine
-
uncompetitive reversible potent IDO-1 inhibitor
beta-carboline
-
-
beta-Methyl-DL-tryptophan
-
1 mM, 7% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
CO
-
negatively cooperative
CO
-
reversed by illumination
cyanide
-
heme ligand, competitive for the ferric enzyme
cyanide
-
prebinding of cyanide to the enzyme facilitates L-Trp binding by 22fold but retards its dissociation by 2fold, indicating that cyanide binding to the heme iron introduces structural changes to the protein matrix allowing faster access of the substrate to the active site and slower dissociation from it. Prebinding of L-Trp to the enzyme retards cyanide binding by about 13fold
cyanide
-
inhibits the dioxygenase activity
D-tryptophan
-
-
dexamethasone
-
inhibits IDO activity in brain and lung after systemic pokeweed mitogen administration and brains of mice suffering from malaria
dexamethasone
-
-
Dichlorophene
-
-
epigallocatechin gallate
-
-
ethyl 1-(4-chlorophenyl)-1H-1,2,3-triazole-4-carboxylate
-
-
exiguamine A
-
inihibor isolated from the marine sponge Neopetrosia exigua
exiguamine A
-
-
exiguamine B
-
-
-
gamma-glutamyl-S-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)cysteinylglycine
-
-
garveatin A
-
-
garveatin C
-
-
garveatin E
-
-
H2O2
-
inhibits the dioxygenase activity in a manner abrogated by L-Trp. Physiological peroxidase substrates, ascorbate or tyrosine, enhanced rIDO-mediated H2O2 consumption and attenuated H2O2-induced protein oxidation and dioxygenase inhibition. H2O2 alters the heme active site of recombinant IDO
hydroxylamine sulfate
-
0.1 mM causes 79% inhibition, 1 mM causes 94% inhibition
imidazole
-
negatively cooperative or competitive
imidodicarbonimidic diamide, N-methyl-N''-9-phenanthrenyl-, monohydrochloride
-
-
indole
-
lowers Km value for D-tryptophan by 60% at pH 7, lowers Vmax by 12-24%, at 1 mM lowers activity by 13%
indole-3-acetic acid
-
1 mM, 19% inhibition of cleavage of D-tryptophan, 27% inhibition of cleavage of L-tryptophan
indole-3-acrylic acid
-
competitive inhibitor
Indole-3-propionic acid
-
-
interleukin-4
-
-
-
iodoacetic acid
-
1 mM, 12% inhibition of cleavage of D-tryptophan, 7% inhibition of cleavage of L-tryptophan
Jatrorrhizine
-
irreversible potent IDO-1 inhibitor
KCN
-
0.01 mM, 39% inhibition of cleavage of D-tryptophan, 48% inhibition of cleavage of L-tryptophan
L-tryptophan
-
substrate inhibition at concentrations above 0.04 mM
L-tryptophan
-
substrate inhibition
L-tryptophan
-
substrate inhibition at 0.14 mM and greater
L-tryptophan
-
substrate inhibition
L-tryptophan
-
substrate inhibition of IDO1, not of IDO2
L-tryptophan ethyl ester
-
1 mM, 7% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
L-tryptophan methyl ester
-
1 mM, 30% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
menadione
-
menadione effectively inhibits L-Trp oxidation from reactions supported with ascorbaic acid/methylene blue
menadione
-
-
methyl 2-methyl-5,10-dioxo-5,10-dihydro-2H-benzo[g]chromene-2-carboxylate
-
-
methyl 4-[(carbamimidoylsulfanyl)methyl]benzenesulfinate hydrobromide
-
-
methyl N-(4-chlorophenyl)carbamimidothioate hydroiodide
-
-
methyl N-[2-(4-chlorophenyl)ethyl]carbamimidothioate hydroiodide
-
-
methyl thiohydantoin-Trp
F5H5G0, P14902
;
-
methyl-thiohydantoin tryptophan
-
-
methyl-thiohydantoin-L-tryptophan
-
competitive inhibitor
-
methyl-thiohydantoin-tryptophan
-
limited selectivity towards indoleamine 2,3-dioxygenase
methylene blue
-
addition of methylene blue (0-0.1 mM) to NADPH-cytochrome P450 reductase-supported D-Trp incubations (with or without cytochrome b5) leads to concentration-dependent inhibition of IDO activity, addition of methylene blue (0-0.03 mM) to NADPH-cytochrome P450 reductase-supported L-Trp oxidation reactions results in a switch from substrate inhibition kinetics to Michaelis-Menten with increasing methylene blue concentration decreasing the affinity of IDO for L-Trp
methylthiohydantoin-DL-tryptophan
-
-
N,N-dimethyl-1-[(4-phenyl-1,3-thiazol-2-yl)sulfanyl]methanamine
-
-
N-(1,3-benzodioxol-5-yl)-2-([5-(4-methylphenyl)[1,3]thiazolo[2,3-c][1,2,4]triazol-3-yl]sulfanyl)acetamide
F5H5G0, P14902
a reversible inhibitor of IDO1. highly specific for IDO1 compared to IDO2, docking analysis with IDO1 and IDO2; a reversible inhibitor of IDO1. highly specific for IDO1 compared to IDO2, docking analysis with IDO1 and IDO2
-
N-(4-hydroxy-1-naphthyl)ethane-1,2-diaminium chloride
-
-
-
N-(4-hydroxy-1-naphthyl)propane-1,3-diaminium chloride
-
-
-
N-(4-hydroxynaphthalen-1-yl)pyrrolidine-2-carboxamide
-
-
N-acetyl-L-tryptophan
-
1 mM, 7% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
n-butyl isocyanide
-
heme ligand which binds tightly to the ferrous enzyme
N-carbamoyl-2-([5-(4-methylphenyl)[1,3]thiazolo[2,3-c][1,2,4]triazol-3-yl]sulfanyl)acetamide
F5H5G0, P14902
poor inhibitor; poor inhibitor
-
N-ethylmaleimide
-
1 mM, 58% inhibition of cleavage of D-tryptophan, 45% inhibition of cleavage of L-tryptophan
N-methyl-L-Trp
F5H5G0, P14902
;
-
N-phenyl-p-phenylenediamine
-
-
NaN3
-
10 mM, 33% inhibition of cleavage of D-tryptophan, 32% inhibition of cleavage of L-tryptophan
naphthalene-1,4-diol
-
-
naphthalene-1,4-dione
-
-
nitric oxide
-
nitric oxide can potentially inhibit isozyme IDO2 activity
NO
-
inhibits the transcription of IDO in murine macrophages
NO
-
can inhibit hIDO by directly binding to the heme iron
NO
-
inhibits activity reversibly by binding to the active site heme to trap the enzyme as an inactive nitrosyl-FeII enzyme adduct with Trp bound and O2 displaced. Reversible inhibition by NO may represent an important mechanism in controlling the immune regulatory actions of IDO
norharman
-
uncompetitive inhibition, 2 mM, 98% inhibition
norharman
-
non competitive, competitive for the ferric enzyme, 0.1 M potassium phosphate buffer (pH 5.5-8), 0.1 M Tris-HCl buffer (pH 7.5-8), 25C
norharman
-
can bind to the ferric and ferrous enzyme to from a quarternary complex
norharman
-
-
norharman
-
-
NSC 401366
-
competitive with respect to tryptophan
Palmatine
-
irreversible potent IDO-1 inhibitor
phenyl-imidazole
-
an IDO1 inhibitor
-
phenylmethanethiol
-
-
primaquine
-
-
quinolin-8-ol
-
-
serotonin
-
1 mM, 36% inhibition of cleavage of D-tryptophan, 37% inhibition of cleavage of L-tryptophan
sodium 4-chlorobenzenesulfinate
-
-
Sodium azide
-
1 mM causes 20% inhibition
Superoxide dismutase
-
80-98% inhibition
-
Superoxide dismutase
-
can be inhibited by diethyldithiocarbamate
-
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
Tiron
-
1 mM causes 40% inhibition
transforming growth factor-beta
-
inhibits expression in skin and synovial fibroblasts
-
tryptamine
-
0.1 mM, 16% inhibition of cleavage of D-tryptophan, 11% inhibition of cleavage of L-tryptophan
tryptamine
-
-
vitamin K3
-
menadione
[4-(1,4-dioxido-1,2,4-benzotriazin-3-yl)aminobutyl]-(2S)-N-tert-butoxycarbonyl-2-amino-(1-methyl-indole-3-yl)propanamide
-
-
[4-(1-oxido-1,2,4-benzotriazin-3-yl)aminobutyl]-(2S)-N-tert-butoxycarbonyl-2-amino-(1-methyl-indole-3-yl)propanamide
-
-
[5-(1,4-dioxido-1,2,4-benzotriazin-3-yl)aminopentyl]-(2S)-N-tert-butoxycarbonyl-2-amino-(1-methyl-indole-3-yl)propanamide
-
-
[5-(1-oxido-1,2,4-benzotriazin-3-yl)aminopentyl]-(2S)-N-tert-butoxycarbonyl-2-amino-(1-methyl-indole-3-yl)propanamide
-
-
mitomycin C
-
-
additional information
-
not inhibited by indo-3-acetamide, beta-indoylacetonitrile snd 3-beta-indoleacrylic acid
-
additional information
-
not inhibited by superoxide dismutase
-
additional information
-
3-indoleethanol and indole affect the L-tryptophan affinity of the ferrous enzyme, indole enhances affinity of enzyme for cyanide and azide and norharman, L-tryptophan lowers norharman affinity for the ferrous dioxygenase
-
additional information
-
not inhibited by catalase and D-tryptophan
-
additional information
-
not inhibited by 6-nitro-D-tryptophan and indole-nitrogen substituted analogues of trytophan
-
additional information
-
review article sumarizing data of many inhibitors of indoleamine 2,3-dioxygenase
-
additional information
-
sodium butyrate does not inhibit the activity of IDO
-
additional information
-
the traditional Chinese medicinal prescription Oren-gedoku-to significantly inhibits recombinant human IDO-1 activity in vitro
-
additional information
-
not inhibited by 1-methyl-D-tryptophan
-
additional information
F5H5G0, P14902
no inhibition by phenylthiohydantoin-Trp; no inhibition by phenylthiohydantoin-Trp
-
additional information
-
structure-activity relationship and enzyme kinetics of 4-aryl-1H-1,2,3-triazoles as indoleamine 2,3-dioxygenase inhibitors, molecular docking studies, overview. An electron-withdrawing group with low steric hindrance near the NH group of triazoles is necessary for the IDO inhibition. No inhibition by 5-(4-methylphenyl)-1H-1,2,3-triazole, methyl 4-(1H-1,2,3-triazol-5-yl)benzoate, 4-bromo-5-phenyl-1H-1,2,3-triazole, 4-chloro-5-phenyl-1H-1,2,3-triazole, 1H-benzotriazol-1-ol, and 5-(4-bromophenyl)-1H-tetrazole
-
additional information
-
the dioxygenase enzyme activity is inhibited by free radical scavengers. Protection of the dioxygenase enzyme function by L-Trp coincides with its oxidation into oxindolylalanine and kynurenine and the formation of a compound II-type ferryl-oxo heme
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(1H-indol-3-yl)ethanol
-
effector
3-indoleethanol
-
1 mM, enhances activity by 87%
alpha-interferon
-
induces de novo synthesis of IDO, but 2 to 3 orders of magnitude less than gamma-IFN
-
alpha-interferon
-
induces IDO expression in monocytes
-
ascorbate
-
promotes IDO peroxidase turnover by reducing Compound II
ascorbic acid
-
-
bacterial lipopolysaccharide
-
-
-
beta-interferon
-
induces IDO expression in monocytes
-
cortisone
-
subcutaneously
cytochrome b5
-
-
-
cytochrome b5
-
-
-
D-tryptophan
-
2g subcutaneously
diethyldithiocarbamate
-
inhibits superoxide dismutase
gamma-interferon
-
-
-
gamma-interferon
-
induces IDO expression in a dose-dependent manner
-
gamma-interferon
-
-
-
gamma-interferon
-
activates expression of IDO
-
gamma-interferon
-
-
-
gamma-interferon
-
induces de novo synthesis of IDO, 30fold increase in IDO activity
-
gamma-interferon
-
induces IDO expression
-
gamma-interferon
-
induces IDO expression
-
gamma-interferon
-
induces IDO expression
-
hematine
-
-
hydrogen peroxide
-
activates the peroxidase function of IDO to induce protein oxidation and inhibit dioxygenase activity
hyperoxia
-
induces IDO expression in the lung
-
Inosine
-
0.1 mM, increases activity 5fold
L-tryptophan
-
2g subcutaneously
lipopolysaccharide
-
induces IDO expression in monocytes
lipopolysaccharide
-
induces IDO expression in the lung
methylene blue
-
acts as electron mediator from donors to the ferric dioxygenase
methylene blue
-
-
NADPH-cytochrome P450 reductase
-
-
-
paraquat
-
induces IDO expression in the lung
tumor-necrosis-factor-alpha
-
costimulation with gamma-interferon
-
methylene blue
-
-
additional information
-
IDO can bind following substances as ligand in effector binding site: alkyl isocyanides, CN-, F-, N3-, imidazoles, pyridines, formate, benzhydroxamate, phosphines
-
additional information
-
not induced by either tryptophan or glucocorticoid; requires molecular oxygen and superoxide anion
-
additional information
-
reactive oxygen intermediates are dispensable for indoleamine 2,3-dioxygenase activity
-
additional information
-
L-Trp is a poor reductant of IDO compound II
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.062
1-methyl-L-tryptophan
-
-
0.006
5-fluoro-tryptophan
-
-
0.1
5-hydroxy-L-tryptophan
-
H303A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min; V109A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.14
5-hydroxy-L-tryptophan
-
H16A, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.17
5-hydroxy-L-tryptophan
-
K352A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.21
5-hydroxy-L-tryptophan
-
37C, pH 6.5
0.4
5-hydroxy-L-tryptophan
-
wild type, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.44
5-hydroxy-L-tryptophan
-
-
0.68
5-hydroxy-L-tryptophan
-
37C, pH 6.5
0.017
5-hydroxy-tryptophan
-
-
0.113
5-methoxy-DL-tryptophan
-
50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
0.088
5-methyl-DL-tryptophan
-
50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
0.098
5-methyl-tryptophan
-
-
0.056
6-methyl-DL-tryptophan
-
50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
0.0019
D-tryptophan
-
H303A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.0024
D-tryptophan
-
H16A, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.0044
D-tryptophan
-
K352A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.005
D-tryptophan
-
wild type, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.0053
D-tryptophan
-
V109A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.062
D-tryptophan
-
pH 7.5, 37 C, 40 min incubation time
0.159
D-tryptophan
-
pH 7.0, 25C, mutant T342A
0.26
D-tryptophan
-
pH 7.0, 25C, wild-type enzyme
0.66
D-tryptophan
-
pH 7.0, 1 mM indole
0.83
D-tryptophan
-
0.1 M potassium phosphate buffer (pH 6-8), 0.025 mM methylene blue, 0.2 mg catalase, 10 mM ascorbic acid, 50 nM dioxygenase, 25C
0.96
D-tryptophan
-
-
1.3
D-tryptophan
-
pH 7.0, 1 mM 3-indoleethanol
1.57
D-tryptophan
-
-
1.7
D-tryptophan
-
pH 7.0
2.6
D-tryptophan
-
-
2.6
D-tryptophan
-
pH and temperature not specified in the publication
2.87
D-tryptophan
-
-
3.795
D-tryptophan
-
50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
4.676
D-tryptophan
-
-
5
D-tryptophan
-
-
5.2
D-tryptophan
-
37C, pH 6.5
7.3
D-tryptophan
-
37C, pH 6.5
0.00072
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the absence of methylene blue and cytochrome b5, in PBS buffer (pH 7.4), at 37C
0.0015
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the absence of methylene blue and in the presence of 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
0.0017
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0001 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
0.0019
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0001 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
0.0039
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0005 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
0.004
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0005 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
0.0049
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.001 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
0.005
L-tryptophan
-
pH 6.0
0.0054
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.001 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
0.0056
L-tryptophan
-
H16A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.0065
L-tryptophan
-
pH 8.0
0.007
L-tryptophan
-
-
0.0089
L-tryptophan
-
V109A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.009
L-tryptophan
-
pH 7.5
0.0094
L-tryptophan
-
H303A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.01
L-tryptophan
-
pH 7.5, 37 C, 5 min incubation time
0.01
L-tryptophan
-
-
0.0124
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.01 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
0.0129
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.01 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
0.013
L-tryptophan
-
pH 7.0
0.0141
L-tryptophan
F5H5G0, P14902
pH 7.0, 22C, IDO2
0.015
L-tryptophan
-
; in the presence of 5.1 mM 3-indole ethanol
0.015
L-tryptophan
-
pH and temperature not specified in the publication
0.016
L-tryptophan
-
in the presence of 2.5 mM 3-indole ethanol
0.018
L-tryptophan
-
50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
0.018
L-tryptophan
-
-
0.02
L-tryptophan
-
-
0.02
L-tryptophan
-
wild type, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.0201
L-tryptophan
-
K352A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
0.0224
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.03 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
0.0234
L-tryptophan
-
A4T mutant protein
0.0246
L-tryptophan
-
-
0.025
L-tryptophan
-
pH 6.5
0.026
L-tryptophan
-
37C, pH 6.5
0.0279
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.03 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
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 37C
0.028
L-tryptophan
-
IDO1, pH and temperature not specified in the publication, MB assay
0.0281
L-tryptophan
-
-
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 37C
0.029
L-tryptophan
-
IDO1, pH and temperature not specified in the publication, cytochrome b5 assay
0.0296
L-tryptophan
-
R77H mutant protein
0.0342
L-tryptophan
-
R77K mutant protein
0.042
L-tryptophan
-
-
0.05
L-tryptophan
-
pH 6.0
0.074
L-tryptophan
-
37C, pH 6.5
0.119
L-tryptophan
-
pH 7.0, 25C, mutant T342A
0.12
L-tryptophan
-
pH 7.0, 25C, wild-type enzyme
0.1815
L-tryptophan
-
-
0.207
L-tryptophan
-
-
0.21
L-tryptophan
-
-
0.25
L-tryptophan
-
pH 5.5
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 37C
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 37C
0.042
O2
-
-
12
L-tryptophan
-
IDO1, pH and temperature not specified in the publication, MB assay
additional information
additional information
-
kinetics of IDO-catalyzed indole oxidation as supported by H2O2, overview. The rate of disappearance of indole as a function of [H2O2] in the IDOFe3+-catalyzed reaction exhibits Michaelis-Menten behavior, with Km of about 1.1 mM for peroxide [indole]
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.064
1-methyl-L-tryptophan
-
-
0.76
5-fluoro-tryptophan
-
-
0.025
5-hydroxy-tryptophan
-
-
3.78
5-methyl-tryptophan
-
-
0.082
D-tryptophan
-
pH 7.0, 25C, mutant T342A
0.2
D-tryptophan
-
pH 7.0, 25C, wild-type enzyme
3.93
D-tryptophan
-
-
5.9
D-tryptophan
-
-
0.0015
kynurenine
-
LPS-treated mice
0.002
kynurenine
-
-
0.101
L-tryptophan
-
pH 7.0, 25C, mutant T342A
0.87
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the absence of methylene blue and cytochrome b5, in PBS buffer (pH 7.4), at 37C
1
L-tryptophan
F5H5G0, P14902
pH 7.0, 22C, IDO2
1.3
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0001 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
1.4
L-tryptophan
-
-
1.7
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the absence of methylene blue and in the presence of 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
2.2
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0001 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
2.24
L-tryptophan
-
pH 7.0, 25C, wild-type enzyme
2.5
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0005 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
3
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.001 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
3.1
L-tryptophan
-
-
3.2
L-tryptophan
-
in the presence of 2.5 mM 3-indole ethanol
3.4
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0005 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
3.5
L-tryptophan
-
in the presence of 5.1 mM 3-indole ethanol
4.2
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.001 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
6.4
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.01 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
8.1
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.03 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
10
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.01 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
12
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.03 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
2.9
O2
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.5
L-tryptophan
F5H5G0, P14902
pH 7.0, 22C, IDO2
119
70.9
L-tryptophan
F5H5G0, P14902
pH 7.0, 22C, IDO1
119
290
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.03 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
119
490
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.01 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
119
540
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.03 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
119
610
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.001 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
119
640
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0005 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
119
740
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.001 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
119
760
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0001 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37C
119
800
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.01 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
119
850
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0005 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
119
1000
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0001 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
119
1100
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the absence of methylene blue and in the presence of 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37C
119
1200
L-tryptophan
-
NADPH-cytochrome P450 reductase-supported oxidation, in the absence of methylene blue and cytochrome b5, in PBS buffer (pH 7.4), at 37C
119
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000061
(3R,4S and 3S,4R)-4-(butylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.00007
(3S,4S and 3R,4R)-4-(benzylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.000066
(3S,4S)-4-(benzylamino)-3,9-dihydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.1
1-methyl-D-tryptophan
-
pH and temperature not specified in the publication
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 37C
0.068
1-methyl-DL-tryptophan
-
-
0.019
1-methyl-L-tryptophan
-
pH and temperature not specified in the publication
0.032
1-methyl-L-tryptophan
-
-
0.062
1-methyl-L-tryptophan
-
37C, pH 6.5
0.062
1-methyl-L-tryptophan
-
-
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 37C
0.105
1-methyl-L-tryptophan
-
37C, pH 6.5
0.105
1-methyl-L-tryptophan
-
-
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 37C
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 37C
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 37C
0.034
1-Methyltryptophan
-
-
0.0532
1-Methyltryptophan
-
-
0.0089
2-(1H-imidazol-4-yl)phenol
-
-
0.0014
2-hydroxygarveatin E
-
25C, pH 6.5
0.0023
2-hydroxygarvin A
-
25C, pH 6.5
0.0053
3-(1H-imidazol-4-yl)benzenethiol
-
-
0.0048
3-(4H-imidazol-4-yl)benzenethiol
-
-
0.0015
4-amino-1,2,5-oxadiazole-3-carboximidamide
-
-
0.018
5-(2-bromophenyl)-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
0.0145
5-(2-chlorophenyl)-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
0.0225
5-phenyl-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
0.18
6-nitro-L-tryptophan
-
1 mM, competitive inhibition, 52% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37C, 10 min
0.00014
annulin A
-
25C, pH 6.5
0.00069
annulin A
-
25C, pH 6.5
0.00012
annulin B
-
25C, pH 6.5
0.00012
annulin B
-
-
0.215
baicalein
-
pH and temperature not specified in the publication
0.008
Berberine
-
pH and temperature not specified in the publication
0.05
D-tryptophan
-
0.1 M potassium phosphate buffer (pH 6-8), 0.025 mM methylene blue, 0.2 mg catalase, 10 mM ascorbic acid, 50 nM dioxygenase, 25C
0.00021
exiguamine A
-
-
0.0032
garveatin A
-
25C, pH 6.5
0.0012
garveatin C
-
25C, pH 6.5
0.0031
garveatin E
-
25C, pH 6.5
0.0015
imidodicarbonimidic diamide, N-methyl-N''-9-phenanthrenyl-, monohydrochloride
-
-
0.0045
indole-3-acrylic acid
-
against L-tryptophan
0.0068
indole-3-acrylic acid
-
against D-tryptophan
0.176
norharman
-
-
0.69
norharman
-
recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37C
1.08
norharman
-
37C, pH 6.5
1.08
norharman
-
recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37C
1.28
norharman
-
37C, pH 6.5
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 37C
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 37C
0.0018
tenatoprazole
-
IDO2, pH and temperature not specified in the publication
-
0.367
[4-(1,4-dioxido-1,2,4-benzotriazin-3-yl)aminobutyl]-(2S)-N-tert-butoxycarbonyl-2-amino-(1-methyl-indole-3-yl)propanamide
-
-
0.0871
[4-(1-oxido-1,2,4-benzotriazin-3-yl)aminobutyl]-(2S)-N-tert-butoxycarbonyl-2-amino-(1-methyl-indole-3-yl)propanamide
-
-
0.197
[5-(1,4-dioxido-1,2,4-benzotriazin-3-yl)aminopentyl]-(2S)-N-tert-butoxycarbonyl-2-amino-(1-methyl-indole-3-yl)propanamide
-
-
0.0763
[5-(1-oxido-1,2,4-benzotriazin-3-yl)aminopentyl]-(2S)-N-tert-butoxycarbonyl-2-amino-(1-methyl-indole-3-yl)propanamide
-
-
1.6
L-tryptophan
-
inhibition of IDO1, pH and temperature not specified in the publication
additional information
additional information
-
review article sumarizing data of many inhibitors of indoleamine 2,3-dioxygenase
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0035
(2,4-dichlorophenyl)methanethiol
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.0012
(2-chlorophenyl)methanethiol
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.0001
(3,4-dichlorophenyl)methanethiol
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.5
(3-hydroxyphenyl)(phenyl)methanone
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.000512
(3R,4S and 3S,4R)-3-bromo-4-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.000361
(3R,4S and 3S,4R)-3-hydroxy-2,2-dimethyl-4-morpholino-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.00396
(3R,4S and 3S,4R)-3-hydroxy-4-methoxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.000183
(3R,4S and 3S,4R)-4-(allylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.000252
(3R,4S and 3S,4R)-4-(benzylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.00345
(3R,4S and 3S,4R)-4-(benzylthio)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.000082
(3R,4S and 3S,4R)-4-(butylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.0015
(3S,4S and 3R,4R)-3,4-dihydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
alpha-lapachone
0.0011
(3S,4S and 3R,4R)-3-hydroxy-2,2-dimethyl-4-morpholino-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.000976
(3S,4S and 3R,4R)-3-hydroxy-4-methoxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.000186
(3S,4S and 3R,4R)-4-(allylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.000055
(3S,4S and 3R,4R)-4-(benzylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.00109
(3S,4S and 3R,4R)-4-(benzyloxy)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.00212
(3S,4S and 3R,4R)-4-(benzylthio)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.00013
(3S,4S)-4-(butylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.0032
(4-chlorophenyl)methanethiol
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.1
(4-chlorophenyl)methanol
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.0018
(4-fluorophenyl)methanethiol
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.0014
(4-methoxyphenyl)methanethiol
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.0013
(4-methylphenyl)methanethiol
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.00045
(4E,4'E)-4,4'-bis(isopropylimino)-2,2'-binaphthyl-1,1'-(4H,4'H)-dione
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.00052
(4E,4'E)-4,4'-bis(pentan-3-ylimino)-2,2'-binaphthyl-1,1'-(4H,4'H)-dione
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.0002
(E)-4-(isopropylimino)-2-methylnaphthalen-1(4H)-one
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.09
(R)-2-amino-N-(4-hydroxynaphth-1-yl)propanamide
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.00034
(S)-2-amino-5-((R)-1-(carboxymethylamino)-3-(1,4-dihydroxy-3-methylnaphthalen-2-ylthio)-1-oxopropan-2-ylamino)-5-oxopentanoic acid
-
-
0.00088
(S)-2-amino-5-((R)-1-(carboxymethylamino)-3-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-ylthio)-1-oxopropan-2-ylamino)-5-oxopentanoic acid
-
-
0.06
(S)-2-amino-N-(4-hydroxynaphth-1-yl)propanamide
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.0071
1,2-naphthoquinone
-
-
0.00099
1,4-naphtho-quinone
-
-
0.05
1-(1,3-benzothiazol-2-ylsulfanyl)-N,N-dimethylmethanamine
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.1
1-(4-chlorobenzyl)urea
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.1
1-(4-chlorophenyl)methanamine
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.1
1-(4-chlorophenyl)thiourea
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.032
1-benzyl-5-phenyl-1H-imidazole
-
-
0.1
1-[2-(4-chlorophenyl)ethyl]thiourea
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
2.57
1H-benzotriazole
-
pH 6.5, 37C, recombinant enzyme
0.00495
2,2-dimethyl-1a,9b-dihydro-2H-benzo[g]oxireno[c]chromene-4,9-dione
-
pH and temperature not specified in the publication
0.000214
2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
dehydro-alpha-lapachone
0.00434
2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
-
0.00495
2,2-dimethyl-3,4-epoxy-2H-naphtho[2,3-b]pyran-5,10-dione
-
-
0.00028
2,3-dichloro-1,4-naphthoquinone
-
-
0.0004
2,4-dichlorobenzyl carbamimidothioate hydrobromide
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.0053
2-(1H-imidazol-4-yl)benzene-1,3-diol
-
-
0.025
2-(1H-imidazol-4-yl)benzenethiol
-
-
0.0048
2-(1H-imidazol-4-yl)phenol
-
-
0.035
2-(1H-pyrazol-3-yl)phenol
-
-
0.1
2-(2-chlorophenyl)ethyl carbamimidothioate hydrobromide
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.1
2-(3-chlorophenyl)ethyl carbamimidothioate hydrobromide
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.1
2-(4-chlorophenyl)ethanamine
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.057
2-(4-chlorophenyl)ethyl carbamimidothioate hydrobromide
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.25
2-([5-(3-methoxyphenyl)[1,3]thiazolo[2,3-c][1,2,4]triazol-3-yl]sulfanyl)-N-(5-methyl-1,3-thiazol-2-yl)acetamide
F5H5G0, P14902
above, pH 7.0, 22C, IDO1; above, pH 7.0, 22C, IDO2
0.4
2-amino-3-hydroxy-N-(4-hydroxynaphthalen-1-yl)propanamide
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.105
2-amino-N-(4-hydroxynaphth-1-yl)acetamide
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.01
2-chlorobenzyl carbamimidothioate hydrochloride
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.675
2-Hydroxy-1,4-naphthoquinone
-
-
0.05
2-mercaptobenzothiazole
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.00072
2-methoxy-1,4-naphthoquinone
-
-
0.0011
2-methyl-1,4-naphthoquinone
-
-
0.0011
2-methylnaphthalene-1,4-dione
-
pH and temperature not specified in the publication
1
2-phenoxyaniline
-
IC50 above 1.0 mM, in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.017
3,4-dichlorobenzyl carbamimidothioate hydrochloride
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.68
3-(1H-1,2,3-triazol-5-yl)pyridine
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.708
3-(1H-1,2,3-triazol-5-yl)pyridine
-
pH 6.5, 37C, recombinant enzyme
0.825
3-(1H-imidazol-4-yl)benzaldehyde
-
-
0.825
3-(1H-imidazol-4-yl)benzaldehyde
-
pH and temperature not specified in the publication
0.0076
3-(1H-imidazol-4-yl)benzenethiol
-
-
0.041
3-(1H-imidazol-4-yl)benzonitrile
-
-
0.365
3-(1H-imidazol-4-yl)phenol
-
-
0.0077
3-(4H-imidazol-4-yl)benzenethiol
-
-
0.0046
3-chlorobenzyl carbamimidothioate hydrochloride
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.00036
3-hydroxy-2,2-dimethyl-4-(morpholin-4-yl)-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
pH and temperature not specified in the publication
0.00396
3-hydroxy-4-methoxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
pH and temperature not specified in the publication
0.161
3-phenylpyridine
-
-
0.005
4-(1H-1,2,3-triazol-5-yl)pyridine
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
1.2
4-(1H-imidazol-4-yl)phenol
-
-
0.734
4-(2,6-dimethoxyphenyl)-1H-imidazole
-
-
0.003
4-(2-(diethylamino)ethylamino)-1-naphthol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.038
4-(2-(methylthio)phenyl)-1H-imidazole
-
-
0.179
4-(2-fluorophenyl)-1H-imidazole
-
-
0.179
4-(2-fluorophenyl)-1H-imidazole
-
pH and temperature not specified in the publication
0.0125
4-(2-hydroxyethoxy)-1-naphthol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.073
4-(3-(methylthio)phenyl)-1H-imidazole
-
-
0.06
4-(3-fluorophenyl)-1H-imidazole
-
-
0.209
4-(4-(methylthio)phenyl)-1H-imidazole
-
-
0.123
4-(4-fluorophenyl)-1H-imidazole
-
-
0.0025
4-(benzylamino)-1-naphthol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.000055
4-(benzylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
pH and temperature not specified in the publication
0.00025
4-(benzylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
pH and temperature not specified in the publication
0.00013
4-(butylamino)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
pH and temperature not specified in the publication
0.015
4-(cyclohexylamino)-1-naphthol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
1
4-(dimethylamino)naphthalen-1-ol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.016
4-(ethylamino)-1-naphthol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.025
4-(isobutylamino)-1-naphthol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.0025
4-(isopropylamino)-1-naphthol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.0125
4-(methylamino)naphthalen-1-ol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.0035
4-(pent-3-ylamino)-1-naphthol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.1
4-(phenylcarbonyl)benzyl carbamimidothioate hydrobromide
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.1
4-(propan-2-yl)benzyl carbamimidothioate hydrobromide
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.0045
4-(propylamino)-1-naphthol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.004
4-(tert-butylamino)naphthalen-1-ol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.422
4-(thiophen-2-yl)-1H-imidazole
-
-
0.422
4-(thiophen-2-yl)-1H-imidazole
-
pH and temperature not specified in the publication
0.0026
4-(trifluoromethyl)benzyl carbamimidothioate hydrochloride
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.003
4-amino-1-naphthol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.0021
4-amino-N'-hydroxy-N-(3-isopropylphenyl)-1,2,5-oxadiazole-3-carboximidamide
-
-
0.0044
4-amino-N'-hydroxy-N-(3-methoxyphenyl)-1,2,5-oxadiazole-3-carboximidamide
-
-
0.00055
4-amino-N'-hydroxy-N-(3-methylphenyl)-1,2,5-oxadiazole-3-carboximidamide
-
-
0.0032
4-amino-N'-hydroxy-N-phenyl-1,2,5-oxadiazole-3-carboximidamide
-
-
0.0065
4-amino-N-(2-chlorophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
0.000059
4-amino-N-(3-bromo-4-fluorophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
0.000073
4-amino-N-(3-bromophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
0.000067
4-amino-N-(3-chloro-4-fluorophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
0.0014
4-amino-N-(3-chlorophenyl)-1,2,5-oxadiazole-3-carbohydrazonamide
-
-
0.000086
4-amino-N-(3-chlorophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
0.00043
4-amino-N-(3-ethylphenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
0.0005
4-amino-N-(3-fluorophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
0.025
4-amino-N-(3-tert-butylphenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
0.006
4-amino-N-(4-chlorophenyl)-N'-hydroxy-1,2,5-oxadiazole-3-carboximidamide
-
-
1.028
4-bromo-5-(4-methylphenyl)-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
0.0013
4-bromobenzyl carbamimidothioate hydrobromide
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.1
4-chlorobenzenesulfonic acid
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.0019
4-chlorobenzenethiol
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.0022
4-chlorobenzyl carbamimidothioate hydrochloride
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.021
4-chlorobenzyl N,N'-dimethylcarbamimidothioate - 1-chlorotetraoxidane (1:1)
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.019
4-cyanobenzyl carbamimidothioate hydrobromide
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.016
4-ethylbenzyl carbamimidothioate hydrochloride
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.026
4-fluoro-2-(1H-pyrazol-3-yl)phenol
-
-
0.026
4-fluoro-2-(1H-pyrazol-3-yl)phenol
-
pH and temperature not specified in the publication
0.013
4-fluorobenzyl carbamimidothioate hydrochloride
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.4
4-hydroxycarbazole
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
1.371
4-iodo-5-phenyl-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
0.0055
4-methoxy-1-naphthylamine
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.052
4-methoxybenzyl carbamimidothioate hydrochloride
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.03
4-methylbenzyl carbamimidothioate hydrochloride
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.533
4-nitro-5-(4-nitrophenyl)-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
0.011
4-nitrobenzyl carbamimidothioate hydrochloride
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
1
4-phenyl-1,3-thiazol-2-amine
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.05
4-phenyl-1,3-thiazole-2-thiol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.048
4-phenylimidazole
-
-
0.1
4-tert-butylbenzyl carbamimidothioate hydrobromide
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.1
4-[(carbamimidoylsulfanyl)methyl]benzoic acid hydrochloride
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.038
4-[2-(methylsulfanyl)phenyl]-1H-imidazole
-
pH and temperature not specified in the publication
0.073
4-[3-(methylsulfanyl)phenyl]-1H-imidazole
-
pH and temperature not specified in the publication
0.148
5-(2-bromophenyl)-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
0.086
5-(2-chlorophenyl)-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
1.028
5-(2-methoxyphenyl)-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
1.256
5-(4-bromophenyl)-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
0.817
5-(4-chlorophenyl)-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
0.58
5-(4-fluorophenyl)-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
6
5-(4-methoxyphenyl)-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
0.04
5-(ethylamino)quinolin-8-ol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.015
5-(isopropylamino)quinolin-8-ol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.003
5-amino-8-hydroxyquinoline
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.05
5-chloro-1,3-benzothiazole-2(3H)-thione
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.001
5-hydroxy-1,4-naphthoquinone
-
-
0.06
5-phenyl-1H-1,2,3-triazole
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.143
5-phenyl-1H-1,2,3-triazole
-
pH 6.5, 37C, recombinant enzyme
0.00019
6-hydroxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
0.00019
6-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-
pH and temperature not specified in the publication
0.00213
6-methoxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
0.00552
7-hydroxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
0.00302
7-methoxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
0.002
8-hydroxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
pH and temperature not specified in the publication
0.00205
8-hydroxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
0.000933
8-methoxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
0.2
9-fluorenone
-
IC50 above 0.2 mM, in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.000121
9-hydroxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
alpha-caryopterone
1
9-hydroxyfluorene
-
IC50 above 1.0 mM, in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.00292
9-methoxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
-
0.00292
9-methoxy-2,2-dimethyl-2H-benzo[g]chromene-5,10-dione
-
pH and temperature not specified in the publication
1
benzophenone
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.061
benzyl carbamimidothioate hydrochloride
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.0093
Berberine
-
pH and temperature not specified in the publication
0.07
Dichlorophene
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
2
ethyl 1-(4-chlorophenyl)-1H-1,2,3-triazole-4-carboxylate
-
pH 6.5, 37C, recombinant enzyme
0.00088
gamma-glutamyl-S-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)cysteinylglycine
-
pH and temperature not specified in the publication
0.00064
menadione
-
in PBS buffer (pH 7.4), at 37C
0.000247
methyl 2-methyl-5,10-dioxo-5,10-dihydro-2H-benzo[g]chromene-2-carboxylate
-
-
0.1
methyl 4-[(carbamimidoylsulfanyl)methyl]benzenesulfinate hydrobromide
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.1
methyl N-(4-chlorophenyl)carbamimidothioate hydroiodide
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.1
methyl N-[2-(4-chlorophenyl)ethyl]carbamimidothioate hydroiodide
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.0216
methyl thiohydantoin-Trp
F5H5G0, P14902
pH 7.0, 22C, IDO1
-
1
N,N-dimethyl-1-[(4-phenyl-1,3-thiazol-2-yl)sulfanyl]methanamine
-
IC50 above 1.0 mM, in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.003
N-(1,3-benzodioxol-5-yl)-2-([5-(4-methylphenyl)[1,3]thiazolo[2,3-c][1,2,4]triazol-3-yl]sulfanyl)acetamide
F5H5G0, P14902
pH 7.0, 22C, IDO1
-
0.25
N-(1,3-benzodioxol-5-yl)-2-([5-(4-methylphenyl)[1,3]thiazolo[2,3-c][1,2,4]triazol-3-yl]sulfanyl)acetamide
F5H5G0, P14902
above, pH 7.0, 22C, IDO2
-
0.044
N-(4-hydroxy-1-naphthyl)ethane-1,2-diaminium chloride
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.005
N-(4-hydroxy-1-naphthyl)propane-1,3-diaminium chloride
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
-
0.2
N-(4-hydroxynaphthalen-1-yl)pyrrolidine-2-carboxamide
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.25
N-carbamoyl-2-([5-(4-methylphenyl)[1,3]thiazolo[2,3-c][1,2,4]triazol-3-yl]sulfanyl)acetamide
F5H5G0, P14902
above, pH 7.0, 22C, IDO1; above, pH 7.0, 22C, IDO2
-
0.4
N-phenyl-p-phenylenediamine
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.0015
naphthalene-1,4-diol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.00099
naphthalene-1,4-dione
-
pH and temperature not specified in the publication
0.0017
phenylmethanethiol
-
in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.05
primaquine
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.75
quinolin-8-ol
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37C
0.1
sodium 4-chlorobenzenesulfinate
-
IC50 above 0.1 mM, in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid (neutralized with NaOH and HCl), 0.01 mM methylene blue, at 37C
0.001
vitamin K3
-
-
0.0826
methyl thiohydantoin-Trp
F5H5G0, P14902
pH 7.0, 22C, IDO2
-
additional information
additional information
-
review article sumarizing data of many inhibitors of indoleamine 2,3-dioxygenase
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000011
-
pulmonary IDO activity in pneumothorax patients
0.000014
-
pulmonary IDO activity in benign tumor patient
0.000015
-
pulmonary IDO activity in tuberculosis patient
0.000039
-
pulmonary IDO activity in bronchiectasis patient
0.00005
-
pulmonary IDO activity in lung cancer patients
0.000067
-
pulmonary IDO activity in pulmonary abscess patient
0.000192
-
L-tryptophan, Tris-buffer, pH 8.0, 0.0001 mM methylene blue and 0.001 mM each of ATP and Mg2+, 37C, 90 min, no rat-pretreatment
0.000208
-
D-tryptophan, Tris-buffer, pH 8.0, 0.0001 mM methylene blue and 0.001 mM each of ATP and Mg2+, 37C, 90 min, no rat-pretreatment
0.000224
-
D-tryptophan, Tris-buffer, pH 8.0, 0.0001 mM methylene blue and 0.001 mM each of ATP and Mg2+, 37C, 90 min, rat-pretreatment with neomycin
0.000245
-
L-tryptophan, Tris-buffer, pH 8.0, 0.0001 mM methylene blue and 0.001 mM each of ATP and Mg2+, 37C, 90 min, rat-pretreatment with cortisone
0.000256
-
D-tryptophan, Tris-buffer, pH 8.0, 0.0001 mM methylene blue and 0.001 mM each of ATP and Mg2+, 37C, 90 min, rat-pretreatment with cortisone
0.000272
-
L-tryptophan, Tris-buffer, pH 8.0, 0.0001 mM methylene blue and 0.001 mM each of ATP and Mg2+, 37C, 90 min, rat-pretreatment with D-tryptophan
0.000277
-
D-tryptophan, Tris-buffer, pH 8.0, 0.0001 mM methylene blue and 0.001 mM each of ATP and Mg2+, 37C, 90 min, rat-pretreatment with D-tryptophan
0.00033
-
crude extract of human lung slices treated with gamma-IFN
0.000598
-
supernatant, 0.8 mM L-tryptophan, 40 mM ascorbic acid, 0.02 mM methylene blue, 200 units/ml catalase, 100 mM potassium phosphate buffer, pH 6.5, 37C, 30 min
0.01
-
ascending colon, 0.05 mM potassium phosphate buffer (pH 7.5), 0.005 mM methylene blue, 0.01 mM ascorbic acid, 0.003 mM tryptophan, 37C; caecum, 0.05 mM potassium phosphate buffer (pH 7.5), 0.005 mM methylene blue, 0.01 mM ascorbic acid, 0.003 mM tryptophan, 37C
0.011
-
brain, in air, 50 mM potassium phosphate buffer, pH 6.5, 0.025 mM methylene blue, 20 mM ascorbate, 0.05 mM catalase, 0.4 mM L-tryptophan, 37C
0.014
-
brain, in 1.2 atm oxygen, 50 mM potassium phosphate buffer, pH 6.5, 0.025 mM methylene blue, 20 mM ascorbate, 0.05 mM catalase, 0.4 mM L-tryptophan, 37C
0.022
-
sample 14 of 22 cervical mucus sampples, determined by HPLC/UV detection, reaction mixture include 0.025 mM methylene blue, 20 mM ascorbic acid, 0.04 mM L-tryptophan solution, 0.05 ml catalase and 50 mM potassium phosphate buffer (pH 6.5), 30 min, 37C
0.024
-
sample 17 of 22 cervical mucus sampples, determined by HPLC/UV detection, reaction mixture include 0.025 mM methylene blue, 20 mM ascorbic acid, 0.04 mM L-tryptophan solution, 0.05 ml catalase and 50 mM potassium phosphate buffer (pH 6.5), 30 min, 37C
0.04
-
small intestine IV, 0.05 mM potassium phosphate buffer (pH 7.5), 0.005 mM methylene blue, 0.01 mM ascorbic acid, 0.003 mM tryptophan, 37C
0.05
-
small intestine proximal portion, 0.05 mM potassium phosphate buffer (pH 7.5), 0.005 mM methylene blue, 0.01 mM ascorbic acid, 0.003 mM tryptophan, 37C
0.07
-
brain, in 5.2 atm oxygen, 50 mM potassium phosphate buffer, pH 6.5, 0.025 mM methylene blue, 20 mM ascorbate, 0.05 mM catalase, 0.4 mM L-tryptophan, 37C
0.07
-
small intestine V, 0.05 mM potassium phosphate buffer (pH 7.5), 0.005 mM methylene blue, 0.01 mM ascorbic acid, 0.003 mM tryptophan, 37C
0.07
-
esophagus
0.072
-
assuming an average wet weight of the lens of 0.2 g, assay in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg/ml catalase, 0.4 mM L-tryptophan, 90 min, 37C
0.08
-
appendix, 0.05 mM potassium phosphate buffer (pH 7.5), 0.005 mM methylene blue, 0.01 mM ascorbic acid, 0.003 mM tryptophan, 37C
0.122
-
submandibular gland
0.13
-
testis
0.145
-
small intestine, in 5.2 atm oxygen, 50 mM potassium phosphate buffer, pH 6.5, 0.025 mM methylene blue, 20 mM ascorbate, 0.05 mM catalase, 0.4 mM L-tryptophan, 37C
0.15
-
appendix, 0.05 mM potassium phosphate buffer (pH 7.5), 0.005 mM methylene blue, 0.01 mM ascorbic acid, 0.003 mM tryptophan, 37C
0.155
-
kidney
0.165
-
brain
0.183
-
heart
0.198
-
lung, in air, 50 mM potassium phosphate buffer, pH 6.5, 0.025 mM methylene blue, 20 mM ascorbate, 0.05 mM catalase, 0.4 mM L-tryptophan, 37C
0.232
-
brain, lipopolysaccharide-treated mice
0.24
-
small intestine, in 1.2 atm oxygen, 50 mM potassium phosphate buffer, pH 6.5, 0.025 mM methylene blue, 20 mM ascorbate, 0.05 mM catalase, 0.4 mM L-tryptophan, 37C
0.24
-
kidney, lipopolysaccharide-treated mice
0.278
-
esophagus, lipopolysaccharide-treated mice
0.342
-
submandibular gland, lipopolysaccharide-treated mice
0.375
-
stomach
0.38
-
small intestine, in air, 50 mM potassium phosphate buffer, pH 6.5, 0.025 mM methylene blue, 20 mM ascorbate, 0.05 mM catalase, 0.4 mM L-tryptophan, 37C
0.425
-
thymus
0.45
-
lung
0.468
-
cecum
0.474
-
sample 11 of 22 cervical mucus sampples, determined by HPLC/UV detection, reaction mixture include 0.025 mM methylene blue, 20 mM ascorbic acid, 0.04 mM L-tryptophan solution, 0.05 ml catalase and 50 mM potassium phosphate buffer (pH 6.5), 30 min, 37C
0.479
-
sample 19 of 22 cervical mucus sampples, determined by HPLC/UV detection, reaction mixture include 0.025 mM methylene blue, 20 mM ascorbic acid, 0.04 mM L-tryptophan solution, 0.05 ml catalase and 50 mM potassium phosphate buffer (pH 6.5), 30 min, 37C
0.55
-
25C, 50 mM HEPES/NaOH (pH 7.3), 5 mM D-tryptophan 0.01 mM methylene blue, 5 mM ascorbic acid, 0.001 mM catalase
0.56
-
testis, lipopolysaccharide-treated mice
0.57
-
heart, lipopolysaccharide-treated mice
0.636
-
sample 15 of 22 cervical mucus sampples, determined by HPLC/UV detection, reaction mixture include 0.025 mM methylene blue, 20 mM ascorbic acid, 0.04 mM L-tryptophan solution, 0.05 ml catalase and 50 mM potassium phosphate buffer (pH 6.5), 30 min, 37C
0.689
-
sample 21 of 22 cervical mucus sampples, determined by HPLC/UV detection, reaction mixture include 0.025 mM methylene blue, 20 mM ascorbic acid, 0.04 mM L-tryptophan solution, 0.05 ml catalase and 50 mM potassium phosphate buffer (pH 6.5), 30 min, 37C
0.72
-
seminal vesicle
0.735
-
trachea, lipopolysaccharide-treated mice
0.755
-
spleen, lipopolysaccharide-treated mice
0.8
-
thymus, lipopolysaccharide-treated mice
0.873
-
lung, in 5.2 atm oxygen, 50 mM potassium phosphate buffer, pH 6.5, 0.025 mM methylene blue, 20 mM ascorbate, 0.05 mM catalase, 0.4 mM L-tryptophan, 37C
0.903
-
colon
0.905
-
lung, in 1.2 atm oxygen, 50 mM potassium phosphate buffer, pH 6.5, 0.025 mM methylene blue, 20 mM ascorbate, 0.05 mM catalase, 0.4 mM L-tryptophan, 37C
0.913
-
sample 13 of 22 cervical mucus sampples, determined by HPLC/UV detection, reaction mixture include 0.025 mM methylene blue, 20 mM ascorbic acid, 0.04 mM L-tryptophan solution, 0.05 ml catalase and 50 mM potassium phosphate buffer (pH 6.5), 30 min, 37C
0.92
-
spleen
0.968
-
trachea
1.39
-
urinary bladder, lipopolysaccharide-treated mice
1.455
-
urinary bladder
1.902
-
stomach, lipopolysaccharide-treated mice
2.017
-
intestine
2.13
-
25C, 50 mM HEPES/NaOH (pH 7.3), 2 mM L-tryptophan 0.01 mM methylene blue, 5 mM ascorbic acid, 0.001 mM catalase
2.48
-
kynurenine, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.2 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 10-60 min
2.67
-
kynurenine, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.2 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37C, 60 min
4.07
-
intestine, lipopolysaccharide-treated mice
5.19
-
small intestine VI, 0.05 mM potassium phosphate buffer (pH 7.5), 0.005 mM methylene blue, 0.01 mM ascorbic acid, 0.003 mM tryptophan, 37C
5.34
-
lung, lipopolysaccharide-treated mice
6.97
-
small intestine distal portion, 0.05 mM potassium phosphate buffer (pH 7.5), 0.005 mM methylene blue, 0.01 mM ascorbic acid, 0.003 mM tryptophan, 37C
8.33
-
seminal vesicle, lipopolysaccharide-treated mice
15.31
-
cecum, lipopolysaccharide-treated mice
26.68
-
colon, lipopolysaccharide-treated mice
32.22
-
epididymis
104.9
-
epididymis, lipopolysaccharide-treated mice
234
-
enzyme after purification, 0.05 mM potassium phosphate buffer (pH 7.5), 0.005 mM methylene blue, 0.01 mM ascorbic acid, 0.003 mM tryptophan, 37C
additional information
-
0.0142 nmol/mg/lens, assay in 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg/ml catalase, 0.4 mM L-tryptophan, 90 min, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 6.5
-
isozyme IDO1
6 - 6.5
-
IDO1
6.5
-
L-tryptophan
6.5
-
L-tryptophan
6.5
-
assay at
6.6 - 6.8
-
in 50 mM phosphate buffer
7 - 8
-
-
7
-
assay at
7
F5H5G0, P14902
assay at; assay at
7.3
-
25C
7.4 - 7.5
-
isozyme IDO2
7.4 - 7.5
-
IDO2
7.4
-
assay at
7.5
-
D-tryptophan
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
-
pH 5.0: about 50% of maximal activity, pH 7.0: about 65% of maximal activity
5 - 7.5
-
pH 5.0: about 50% of maximal activity, pH 7.5: about 65% of maximal activity
5.5 - 8
-
5% activity loss at pH 5.5, 10% activity loss at pH 7, 20% activity loss at pH 8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
F5H5G0, P14902
assay at room temperature; assay at room temperature
25
-
assay at
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.09
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
marrow stromal cell or mesenchymal stem cells (MSC)
Manually annotated by BRENDA team
-
microvascular endothelial cell, HBMEC
Manually annotated by BRENDA team
-
in the group of rats aged 12 months, the highest specific activity is found in the small intestine
Manually annotated by BRENDA team
-
IDO-1 is associated with senile plaques in Alzheimer's disease brains and is specifically localized in conjunction with neurofibrillary tangles
Manually annotated by BRENDA team
-
from humans suffering from inflammatory neurological disorders exhibit increased IDO activity
Manually annotated by BRENDA team
-
very irregular activity
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
IDO-competent cells exhibit attributes of B cells as well as dendritic cells
Manually annotated by BRENDA team
-
in glandular epithelium in first trimester pregnancy
Manually annotated by BRENDA team
-
strong expression in stromal and glandular epithelial cells of the first trimester decidua
Manually annotated by BRENDA team
-
tumor-associated dendritic cell, indoleamine 2,3-dioxygenase is up-regulated after maturation of dendritic cells in presence of prostaglandin E2
Manually annotated by BRENDA team
-
expressed in antigen-presenting dendritic cells where tryptophan catabolism drives immune tolerance
Manually annotated by BRENDA team
-
mature, but not immature dendritic cells metabolize tryptophan
Manually annotated by BRENDA team
-
arterially derived, express little indoleamine 2,3-dioxygenase, which is poorly upregulated upon activation (except by mycoplasma)
Manually annotated by BRENDA team
-
IDO1 is constitutively expressed in the epididymis
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
i.e. human umbilical vein endothelial cell, express little indoleamine 2,3-dioxygenase, which is poorly upregulated upon activation (except by mycoplasma)
Manually annotated by BRENDA team
-
in HUVEC cells the enzyme is upregulated by incubation with cytokines or in mycoplasma-infected cells. Inhibition of indoleamine 2,3-dioxygenase improves ability of HUVEC cells to stimulate T-cell proliferation
Manually annotated by BRENDA team
-
IDO is highly expressed throughout the intestine with a marked presence in the jejunum and ileum both at the RNA and protein level
Manually annotated by BRENDA team
-
intestinal mucosa of rat exhibits lower activity than in rabbit
Manually annotated by BRENDA team
-
intestinal biopsies from patients with coeliac disease show an increased expression of indoleamine 2,3-dioxygenase
Manually annotated by BRENDA team
-
IDO is highly expressed throughout the intestine with a marked presence in the jejunum and ileum both at the RNA and protein level
Manually annotated by BRENDA team
-
IDO is highly expressed throughout the intestine with a marked presence in the jejunum and ileum both at the RNA and protein level
Manually annotated by BRENDA team
-
low activity in rats aged 2-3 months or 12 months
Manually annotated by BRENDA team
Q8R0V5
tubular cells in the kidney
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
anterior and bow region
Manually annotated by BRENDA team
-
upregulation of IDO in the livers of chimpanzees with chronic hepatitis C
Manually annotated by BRENDA team
-
upregulation of IDO in the livers of patients with chronic hepatitis C
Manually annotated by BRENDA team
-
cancer bearing lung exhibits 20fold increase in IDO activity
Manually annotated by BRENDA team
-
low activity, activity is not age-related
Manually annotated by BRENDA team
-
induced by alpha-, beta- and gamma-interferon
Manually annotated by BRENDA team
-
the enzyme is upregulated by interferon-gamma in neurons of the hippocampus. The enzyme could contribute to the vulnerability of neurons to inflammatory conditions
Manually annotated by BRENDA team
-
K562 from human erythroleukemia, human hepatocellular carcinoma cell line HepG2
Manually annotated by BRENDA team
Mus musculus DBA/2J
-
-
-
Manually annotated by BRENDA team
-
term placenta
Manually annotated by BRENDA team
-
brush border microvillous plasma membranes of placental syncytiotrophoblast
Manually annotated by BRENDA team
-
in the first and second trimester placenta the enzyme is localized to the syncytiotrophoblast, stroma and macrophages. In term placenta confined mainly to vascular endothelial cells of villous blood vessels, and to macrophages within the fetal villus
Manually annotated by BRENDA team
-
in newborn rats IDO activity is present only in small intestine. In the group of rats aged 2-3 months, the highest specific activity is found in the small intestine, decrease of enzyme activity in relation to age
Manually annotated by BRENDA team
-
dentritic cells
Manually annotated by BRENDA team
Mus musculus DBA/2J
-
dentritic cells
-
Manually annotated by BRENDA team
-
IDO-competent cells are present in spleens of B-cell-deficient mice
Manually annotated by BRENDA team
-
peritumoral infiltrate
Manually annotated by BRENDA team
-
brush border microvillous plasma membranes of placental syncytiotrophoblast
Manually annotated by BRENDA team
-
monocytes are a major source of active IDO in normal peripheral blood
Manually annotated by BRENDA team
additional information
-
endometrial glandular and surface epithelial cells exhibit strong activity during the secretory phase
Manually annotated by BRENDA team
additional information
-
entorhinal cortex
Manually annotated by BRENDA team
additional information
-
T-lymphocyte
Manually annotated by BRENDA team
additional information
-
analysis of various tissues
Manually annotated by BRENDA team
additional information
-
IDO is found ubiquitously in all tissues
Manually annotated by BRENDA team
additional information
-
IDO is not detected in CD103- gut dendritic cells and in spleen
Manually annotated by BRENDA team
additional information
-
IDO1 expression is found in most tissues and is regulated by immunological signals, including interferon-gamma, lipopolysaccharide and tumor necrosis factor
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Mus musculus DBA/2J
-
-
-
Manually annotated by BRENDA team
additional information
-
expressed in epithelial cells but not in mature fiber cells
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42000
-
SDS-PAGE
712172
42000
-
SDS-PAGE
713591
43000
-
gel filtration, lung
666763
43000
-
SDS-PAGE
712173
45000
-
SDS-PAGE
395469, 659233, 666378
45000
-
isozymes IDO1 and IDO2, SDS-PAGE
710831
45200
-
isozyme IDO2, calculated from amino acid sequence
710831
45300
-
isozyme IDO1, calculated from amino acid sequence
710831
45440
-
ESI mass spectrometry
395463
46980
-
ESI mass spectrometry
395463
150000
-
alpha2beta2 subunit
663910
320000
-
gel filtration, liver
666763
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 45000
?
-
x * 45000-50000, SDS-PAGE
?
-
x * 45000, calculated from sequence
monomer
-
-
monomer
-
1 * 45000
monomer
-
x-ray crystallography
monomer
-
about 45000 Da
monomer
-
1 * 42000-45000
monomer
-
1 * 45000, isozymes IDO1 and IDO2, SDS-PAGE
monomer
-
x * 45000, about, IDO2, SDS-PAGE
monomer
-
x * 47000, about, IDO2, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, crystal structure of the enzyme complexed with the ligand inhibitor 4-phenylimidazole and cyanide and cyanide at resolutions of 2.3 and 3.4 A respectively
-
sitting-drop vapour-diffusion method. Crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 86.1, b = 98.0, c = 131.0 A. 2.3 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-20
-
losing 70% activity after 24 h, addition of 5 mg/ml BSA maintaines 80% activity after 5 days
666239
4
-
maintaines 70% activity with addition of 2 mg/ml catalase for 4 days
666239
48 - 60
-
the melting temperature of the denaturation process for recombinant isozyme IDO1 is 60C, with a possible second intermediate at 48C, recombinant isozyme IDO2 denatures in a single step, with a melting temperature at 48C
710831
48
-
complete denaturation of IDO2, partially of IDO1
723923
60
-
complete denaturation of IDO1
723923
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
highly autoxidizable, requires superoxide anion or a reductant such as ascorbic acid and methylene blue as cofactors
-
663996
leuco-methylene blue reduces ferric enzyme
-
395458
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, losing 70% activity after 24 h, addition of 5 mg/ml bovine serum albumin maintains 80% activity after 5 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
0-5C, homogenization, Protein G-Sepharose
-
cryosections deparaffinized, rehydrated, cooked in 0.01 M citrate buffer (pH 6.0), incubated with IDO antibody at room temperature for 30 min
-
HisTrap column chromatography and Superdex 200 gel filtration
-
homogenization, filtered through cotton gauze, centrifugation, collection, stored at -20C
-
IMAC nickel affinity column chromatography
-
Ni-NTA-agarose and gel filtration (Superdex 75)
-
phosphocellulose and Ni-NTA-agarose affinity chromatography
-
recombinant
-
recombinant enzyme from Escherichia coli involving affinity chromatography
-
recombinant His6-tagged IDO1 from Escherichia coli strain BL21 Star by nickel affinity chromatography and gel filtration; recombinant His6-tagged IDO2 from Escherichia coli strain BL21 Star by nickel affinity chromatography and gel filtration
F5H5G0, P14902
tissues thawed at room temperature, homogenized in 0.14 M potassium chloride plus 20 mM potassium phosphate, pH 7.0
-
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
-
homogenization, ammonium sulfate precipitation, gel filtration with Sephacryl S200, Bio-gel HT column, stored at -75C
-
homogenization, ammonium sulfate precipitation
-
dialysis, lyophilization
-
tissues thawed at room temperature, homogenized in 0.14 M potassium chloride plus 20 mM potassium phosphate, pH 7.0
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
COS-7 cells expressing active human IDO
-
expressed in COS-7 and HEK293 cell, C-terminal hemagglutinin-tagged
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 AI cells
-
expressed in Escherichia coli BL21 Star cells
-
expressed in Mus musculus
-
expression in Escherichia coli
-
expression in Escherichia coli E538, expressed with His-Tag
-
expression in Escherichia coli E538, formation of inclusion bodies at 37C with reduced formation, at 30C, expressed with His-Tag
-
expression in Escherichia coli strain YA21
-
expression in Saccharomyces cerevisiae tryptophan auxotroph can restore growth in presence of low tryptophan concentrations
-
expression of His6-tagged IDO1 in Escherichia coli strain BL21 Star; expression of His6-tagged IDO2 in Escherichia coli strain BL21 Star
F5H5G0, P14902
large scale expression in Escherichia coli
-
N-terminal His tag, expressed in Escherichia coli
-
recombinant expression in Escherichia coli
-
isozyme IDO2 is expressed in KRX cells, isozyme IDO1 is expressed in Escherichia coli Rosetta cells
-
large scale expression in Escherichia coli
-
expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
IDO expression is negatively regulated by interleukin-4, nitric oxide and transforming growth factor-beta
-
sodium butyrate down-regulates indoleamine 2,3-dioxygenase at the transcriptional and post-transcriptional levels. Treatment with sodium butyrate (up to 0.2 mM) significantly reduces IDO induction, which is almost completely inhibited at a concentration of 0.5 mM. Sodium butyrate causes a ubiquitin-mediated proteasomal degradation process that contributes to degradation of IDO. Treatment with bortezomib significantly represses sodium butyrate-induced down-regulation of IDO protein
-
IDO expression is not induced by interferon-alpha
-
IDO activity is increased during severe sepsis and septic shock and is associated with mortality. IDO activity is maximal in culture after 3 days of interferon-gamma stimulation
-
IDO expression is induced by interferon-gamma. IDO is detected when exposed to 100 units/ml IFN-gamma for 4 h and is enhanced by continuous exposure to IFN-gamma
-
IDO expression is positively regulated by interferon-gamma, CD40 ligand, COX-2, lipopolysaccharide, tumor necrosis factor-alpha, and hepatocyte growth factor
-
IDO is an interferon-gamma-induced enzyme
-
IDO-1 levels are increased in Alzheimer's disease brains compared to controls
-
interferon-gamma induces the expression of indoleamine 2,3-dioxygenase, an 100fold and 200fold increase in IDO activity is detected with IFN-gamma concentrations of 5 and 10 units/ml, respectively
-
TLR9 ligand CpG, soluble CTLA4 or interferon-gamma induce IDO expression
-
treatment with 1000 units/ml interferon-gamma increases the PDL-1 cell surface expression and the IDO activity
-
treatment with 25 ng HIV-1 clade B Tat protein significantly upregulates IDO gene and protein expression 24 h after incubation compared to HIV-1 clade C Tat protein
-
IDO1 expression is upregulated by cytokines such as IFN-gamma, e.g. in HELA cells, IDO2 mRNA expression is upregulated in response to IFN-gamma in some cancer cell lines as well and human mesenchymal stem cells
-
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
-
IDO expression in bone marrow-derived dendritic cells is increased by hemin, a potent inducer of heme oxygenase-1
-
isozyme IDO 1 (but not isozyme IDO2) is induced specifically in the lungs of mice infected with Francisella novicida or Streptococcus pneumonia
-
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
-
treatment with interferon-gamma (200 units/ml) induces expression of IDO
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A4T
-
variant observed in Homo sapiens
D274A
-
mutant without enzyme activity, may be distal ligand or essential in maintaining the conformation of the heme pocket
F226A
-
drastically reduced the dioxygenase activity
F227A
-
drastically reduced the dioxygenase activity
H16A
-
does not act as proximal ligand
H303A
-
does not act as proximal ligand
H303A
-
Fe3+/Fe2+ reduction potential of H303A variant is about 70 mV lower than that of recombinant wild-type enzyme, leading to a destabilization of the ferrous-oxy complex
H346A
-
mutant without enzyme activity, His346 is essential for heme binding
K352A
-
mutant with diminished heme binding ability
R231A
-
drastically reduced the dioxygenase activity
R77H
-
variant observed in Homo sapiens
R77K
-
variant not observed in Homo sapiens, used as control
S167H
-
the ferrous-oxy complex is dramatically destabilized in this variant
S167H
-
active site, mimic tryptophan 2,3-oxigenase
S263A
-
activity is reduced to 15%
T342A
-
site-directed mutagenesis, the mutation only slightly perturbs the global structural properties of the enzyme, but it totally abolishes the substrate stereoselectivity, substrate-free spectrum
V109A
-
mutant maintained heme binding ability
medicine
-
IDO expression as a T-cell inhibitory effector pathway in professional antigen-presenting cells
additional information
-
in a 9 bp-deletion variant (observed in Homo sapiens) 4 amino acid residues (199-202: ALLE) are replaced by D, variant L197I observed in Homo sapiens
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
the enzyme is a promising therapeutic target of cancer
drug development
F5H5G0, P14902
therapeutic inhibition of IDO1 is receiving much attention due to its proposed role in the pathogenesis of several diseases including cancer, hypotension and neurodegenerative disorders
medicine
-
enzyme catalyzes the first and rate-limiting step in kynurenine pathway
medicine
-
first and probably rate-limiting enzyme in UV filter biosynthesis
medicine
-
first and rate-limiting enzyme in tryptophan metabolism, plas a role in pathogenesis of many diseases
medicine
-
first and rate-limiting enzyme in tryptophan metabolism, plays a role in pathogenesis of many diseases
medicine
-
IDO induces suppression of antitumoral immune response, inhibits tumor cell proliferation by tryptophan depletion
medicine
-
inhibits T-cell activation and proliferation
medicine
-
plays a role in the antiparasitic defense in humans
medicine
-
plays a role in the antiparasitic defense in humans, inhibits the growth of tumor cell lines in vitro, inhibits T lymphocyte proliferation
medicine
-
in patients with acute myeloid leukemia, activity of indoleamine 2,3-dioxygenase can be monitored by measuring its metabolites in sera, and appears correlated with outcome. Monitoring indoleamine 2,3-dioxygenase activity provides a useful tool for future clinical trials of IDO inhibitors in acute myeloid leukemia
medicine
-
the IDO enzyme is involved in the immune regulation of early atherosclerosis, particularly in young female adults, and could constitute a novel marker of immune activation in early atherosclerosis in females
medicine
-
identification of genetic variants, which have altered enzyme activity
medicine
-
indole 2,3-dioxygenase acitvity in bacteremic patients
medicine
-
indole 2,3-dioxygenase is potentially useful as a non-invasive marker for organ transplant rejection
medicine
-
review of multifaceted activity of indole 2,3-dioxygenase in infections
medicine
-
genetic alteration of fetal IDO gene is not a primary cause of pre-eclampsia
pharmacology
-
first reaction in the tryptophan catabolic pathway in mammals
medicine
-
reduced tryptophan and increased kynurenine concentrations, chronic immune activation which can be referred to increased IDO activation
medicine
-
rate-limiting enzyme in kynurenine pathway
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
medicine
-
rate-limiting enzyme in kynurenine pathway
medicine
-
engraftment of IDO expressing skin substitutes on the back of rats significantly improves healing progression over 7 days compared with both nontreated and non-IDO-expressing skin substitutes