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(1R,2S)-2-([[6-(trifluoromethyl)-1H-indazol-4-yl]amino]methyl)cyclohexan-1-ol
-
-
(1R,2S)-2-[[(5-bromo-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
-
-
(1R,2S)-2-[[(5-bromo-1H-indazol-7-yl)amino]methyl]cyclohexan-1-ol
-
-
(1R,2S)-2-[[(5-chloro-1H-indazol-7-yl)amino]methyl]cyclohexan-1-ol
-
-
(1R,2S)-2-[[(6-bromo-1-methyl-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
-
-
(1R,2S)-2-[[(6-bromo-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
-
-
(1R,2S)-2-[[(6-bromo-1H-indazol-4-yl)amino]methyl]cyclohexyl acetate
-
-
(1R,2S)-2-[[(6-chloro-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
-
-
(1R,2S)-2-[[(6-methyl-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
-
-
(1S,2R)-2-[[(6-bromo-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
-
-
(2E)-3-(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)prop-2-enoic acid
-
-
(4-phenyl-1,2-oxazol-5-yl)methanol
-
-
(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)boronic acid
-
-
1-(2-hydroxy-4-methylphenyl)-3-(2-methoxyphenyl)propane-1,3-dione
-
-
1-(2-hydroxy-4-methylphenyl)-3-{2-[(propan-2-yl)oxy]phenyl}propane-1,3-dione
-
-
1-(2-methylbenzyl)-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
-
1-(3-bromobenzyl)-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
-
1-(3-bromothiophen-2-yl)-2-(3-methyl-1,4-dihydronaphthalen-2-yl)ethan-1-one
most potent inhibitor capable of blocking both indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO2) activity, with the IC50 value for BT-549 cells at 0.00342 mM
-
1-(3-chlorobenzyl)-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
-
1-(3-[(4-acetyl-1-piperazinyl)carbonyl]benzyl)-1H-naphtho-[2,3-d][1,2,3]triazole-4,9-dione
-
1-(3-[(4-methyl-1-piperazinyl)carbonyl]benzyl)-1H-naphtho-[2,3-d][1,2,3]triazole-4,9-dione
-
1-(4-bromobenzyl)-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
-
1-(4-fluorobenzyl)-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
-
1-(4-methylbenzyl)-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
-
1-(4-[(4-acetylpiperazin-1-yl)carbonyl]benzyl)-1H-naphtho-[2,3-d][1,2,3]triazole-4,9-dione
-
1-(4-[(4-methoxypiperidin-1-yl)carbonyl]benzyl)-1Hnaphtho[2,3-d][1,2,3]triazole-4,9-dione
-
1-(cyclopropylmethyl)-5-(1H-indol-3-yl)-1H-benzotriazole
-
-
1-(cyclopropylmethyl)-6-(1H-indol-3-yl)-1H-benzotriazole
-
-
1-cyclohexyl-2-(5H-imidazo[5,1-a]isoindol-5-yl)ethan-1-ol
-
1-[(3-methylphenyl)methyl]-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
-
1-[(4-chlorophenyl)methyl]-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
-
1-[(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)methyl]piperidine-3-carboxylic acid
-
-
1-[(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)methyl]piperidine-4-carboxylic acid
-
-
1-[(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)methyl]proline
-
-
1-[3-(4-morpholinylcarbonyl)benzyl]-1H-naphtho[2,3-d]-[1,2,3]triazole-4,9-dione
-
1-[4-(morpholin-4-ylcarbonyl)benzyl]-1H-naphtho[2,3-d]-[1,2,3]triazole-4,9-dione
-
1-[4-[(4-methylpiperazin-1-yl)carbonyl]benzyl]-1H-naphtho-[2,3-d][1,2,3]triazole-4,9-dione
-
2-(4-[(4,9-dioxo-4,9-dihydro-1H-naphtho[2,3-d][1,2,3]-triazol-1-yl)methyl]phenyl)-N,N-diethylacetamide
-
2-[(6-bromo-1H-indazol-4-yl)amino]-1-(3-chlorophenyl)ethan-1-ol
-
-
2-[(6-bromo-1H-indazol-4-yl)amino]-1-(4-hydroxyphenyl)ethan-1-one
-
-
2-[(6-bromo-1H-indazol-4-yl)amino]-2-(3-chlorophenyl)ethan-1-ol
-
-
2-[(6-bromo-1H-indazol-4-yl)amino]-2-phenylethan-1-ol
-
-
2-[5-(1H-indol-3-yl)-1H-benzotriazol-1-yl]-N,N-dimethylethan-1-amine
-
-
2-[5-(1H-indol-3-yl)-1H-benzotriazol-1-yl]acetamide
-
-
2-[6-(1H-indol-3-yl)-1H-benzotriazol-1-yl]-N,N-dimethylethan-1-amine
-
-
2-[6-(1H-indol-3-yl)-1H-benzotriazol-1-yl]acetamide
-
-
2-[[(6-bromo-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
-
-
3-methyl-4-phenyl-1,2-oxazol-5-amine
-
-
3-[(4,9-dioxo-4,9-dihydro-1H-naphtho[2,3-d][1,2,3]triazol-1-yl)methyl]-N,N-diethylbenzamide
-
3-[(4,9-dioxo-4,9-dihydro-1H-naphtho[2,3-d][1,2,3]triazol-1-yl)methyl]benzoic acid
-
3-[5-(1H-indol-3-yl)-1H-benzotriazol-1-yl]propane-1,2-diol
-
-
3-[6-(1H-indol-3-yl)-1H-benzotriazol-1-yl]propane-1,2-diol
-
-
4-(1H-pyrazol-1-yl)-1,2-oxazol-5-amine
-
-
4-(3-chlorophenyl)-1,2-oxazol-5-amine
-
-
4-(3-chlorophenyl)-imidazole
-
-
4-(3-methoxyphenyl)-1,2-oxazol-5-amine
-
-
4-(3-methyl-1H-pyrazol-1-yl)-1,2-oxazol-5-amine
-
-
4-(4-chlorophenyl)-1,2-oxazol-5-amine
-
-
4-(4-fluoro-1H-pyrazol-1-yl)-1,2-oxazol-5-amine
-
-
4-(4-fluorophenyl)-1,2-oxazol-5-amine
-
-
4-(4-methyl-1H-pyrazol-1-yl)-1,2-oxazol-5-amine
-
-
4-(pyridin-2-yl)-1,2-oxazol-5-amine
-
-
4-(pyridin-3-yl)-1,2-oxazol-5-amine
-
-
4-(thiophen-2-yl)-1,2-oxazol-5-amine
-
-
4-(thiophen-3-yl)-1,2-oxazol-5-amine
-
-
4-([[(1S,2R)-2-hydroxycyclohexyl]methyl]amino)-1H-indazole-6-carboxylic acid
-
-
4-chlorophenyl-1,2,3-triazol-4-amine
-
-
4-cyclohexyl-1,2-oxazol-5-amine
-
-
4-cyclopentyl-1,2-oxazol-5-amine
-
-
4-phenyl-1,2-oxazol-5-amine
-
-
4-phenyl-1,2-thiazol-5-amine
-
-
4-[(1Z)-2-[(6-bromo-1H-indazol-4-yl)amino]-N-hydroxyethanimidoyl]phenol
-
-
4-[(4,9-dioxo-4,9-dihydro-1H-naphtho[2,3-d][1,2,3]triazol-1-yl)methyl]-N,N-diethylbenzamide
-
4-[(4,9-dioxo-4,9-dihydro-1H-naphtho[2,3-d][1,2,3]triazol-1-yl)methyl]benzoic acid
-
4-[[(6-bromo-1H-indazol-4-yl)amino]methyl]phenol
-
-
5-(1H-indol-3-yl)-1-(2,2,2-trifluoroethyl)-1H-benzotriazole
-
-
5-(1H-indol-3-yl)-1-methyl-1H-benzotriazol-4-amine
-
-
5-(1H-indol-3-yl)-1-methyl-1H-benzotriazole
-
-
5-(1H-indol-3-yl)-1-[(oxolan-2-yl)methyl]-1H-benzotriazole
-
-
5-(1H-indol-3-yl)-1-[(oxolan-3-yl)methyl]-1H-benzotriazole
-
-
5-(1H-indol-3-yl)-1-[(piperidin-4-yl)methyl]-1H-benzotriazole
-
-
5-(1H-indol-3-yl)-1-[2-(morpholin-4-yl)ethyl]-1H-benzotriazole
-
-
5-(1H-indol-3-yl)-1-[2-(piperazin-1-yl)ethyl]-1H-benzotriazole
-
-
5-(1H-indol-3-yl)-1-[2-(pyrrolidin-3-yl)ethyl]-1H-benzotriazole
-
-
5-(1H-indol-3-yl)-2-methyl-2H-benzotriazol-4-amine
-
-
5-(1H-indol-3-yl)-2-methyl-2H-benzotriazole
-
-
5-(6-fluoro-1H-indol-3-yl)-1-methyl-1H-benzotriazole
-
-
5-(6-fluoro-1H-indol-3-yl)-1-[2-(piperazin-1-yl)ethyl]-1H-benzotriazole
-
-
5-phenyl-1,2,3-thiadiazol-4-amine
potent tryptophan 2,3-dioxygenase 2 inhibitor with modest selectivity over indolamine 2,3-dioxygenase 1 and with improved human whole blood stability
-
6-(1H-indol-3-yl)-1-(2,2,2-trifluoroethyl)-1H-benzotriazole
-
-
6-(1H-indol-3-yl)-1-methyl-1H-benzotriazol-7-amine
-
-
6-(1H-indol-3-yl)-1-methyl-1H-[1,2,3]triazolo[4,5-b]pyridine
-
-
6-(1H-indol-3-yl)-1-methyl-7-nitro-1H-benzotriazole
-
-
6-(1H-indol-3-yl)-1-[(oxolan-2-yl)methyl]-1H-benzotriazole
-
-
6-(1H-indol-3-yl)-1-[(oxolan-3-yl)methyl]-1H-benzotriazole
-
-
6-(1H-indol-3-yl)-1-[(piperidin-4-yl)methyl]-1H-benzotriazole
-
-
6-(1H-indol-3-yl)-1-[(pyrrolidin-3-yl)methyl]-1H-benzotriazole
-
-
6-(1H-indol-3-yl)-1-[2-(morpholin-4-yl)ethyl]-1H-benzotriazole
-
-
6-(1H-indol-3-yl)-1-[2-(piperazin-1-yl)ethyl]-1H-benzotriazole
-
-
6-(1H-indol-3-yl)-1H-benzotriazole
-
-
6-(1H-indol-3-yl)-2-methyl-2H-[1,2,3]triazolo[4,5-b]pyridine
-
-
6-(1H-indol-3-yl)-3-methyl-3H-[1,2,3]triazolo[4,5-b]pyridine
-
-
6-(1H-indol-3-yl)isoquinoline
-
-
6-(1H-indol-3-yl)quinazoline
-
-
6-bromo-1H-indazol-4-amine
-
-
6-bromo-N-(cyclohexylmethyl)-1H-indazol-4-amine
-
-
6-bromo-N-[(1,4-dioxaspiro[4.5]decan-6-yl)methyl]-1H-indazol-4-amine
-
-
6-bromo-N-[(1R,2R)-2-hydroxycyclohexyl]-1H-indazole-4-carboxamide
-
-
6-bromo-N-[(pyridin-2-yl)methyl]-1H-indazol-4-amine
-
-
6-bromo-N-[(pyrrolidin-3-yl)methyl]-1H-indazol-4-amine
-
-
6-bromo-N-[[(1S,2S)-2-chlorocyclohexyl]methyl]-1H-indazol-4-amine
-
-
6-bromo-N-[[(2R)-piperidin-2-yl]methyl]-1H-indazol-4-amine
-
-
6-bromo-N-[[(2R)-pyrrolidin-2-yl]methyl]-1H-indazol-4-amine
-
-
6-bromo-N-[[(2S)-piperidin-2-yl]methyl]-1H-indazol-4-amine
-
-
6-bromo-N-[[(2S)-pyrrolidin-2-yl]methyl]-1H-indazol-4-amine
-
-
6-fluoro-3-[(E)-2-(1H-tetrazol-5-yl)ethenyl]-1H-indole
-
-
6-fluoro-3-[(E)-2-(pyridin-3-yl)ethenyl]-1H-indole
-
-
7-(1H-indol-3-yl)-3,4-dihydroquinazolin-2(1H)-one
-
-
7-(1H-indol-3-yl)isoquinoline
-
-
7-(1H-indol-3-yl)quinazoline
-
-
8-fluoro-2-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)indolo[2,1-b]quinazoline-6,12-dione
-
-
8-fluoro-2-[(1H-1,2,3-triazol-1-yl)methyl]indolo[2,1-b]quinazoline-6,12-dione
-
-
8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazoline-2-carbaldehyde
-
-
ethyl (2E)-3-(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)prop-2-enoate
-
-
isatin
-
mechanism of inhibition
methyl 1-[(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)methyl]piperidine-3-carboxylate
-
-
methyl 1-[(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)methyl]piperidine-4-carboxylate
-
-
methyl 1-[(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)methyl]prolinate
-
-
methyl 4-([[(1S,2R)-2-hydroxycyclohexyl]methyl]amino)-1H-indazole-6-carboxylate
-
-
N-(3-bromo-4-fluorophenyl)-N'-hydroxy-4-[[2-(sulfamoylamino)ethyl]amino]-1,2,5-oxadiazole-3-carboximidamide
-
-
N-(4-[[(6-bromo-1H-indazol-4-yl)amino]methyl]cyclohexylidene)hydroxylamine
-
-
N-methyl-4-phenyl-1,2-oxazol-5-amine
-
-
N-[(azetidin-3-yl)methyl]-6-bromo-1H-indazol-4-amine
-
-
N-[[(1S,2R)-2-aminocyclohexyl]methyl]-6-bromo-1H-indazol-4-amine
-
-
N-[[(1S,2S)-2-aminocyclohexyl]methyl]-6-bromo-1H-indazol-4-amine
-
-
tert-butyl 3-[[(6-bromo-1H-indazol-4-yl)amino]methyl]pyrrolidine-1-carboxylate
-
-
[5-(1H-indol-3-yl)-1H-benzotriazol-1-yl]acetic acid
-
-
[6-(1H-indol-3-yl)-1H-benzotriazol-1-yl]acetic acid
-
-
additional information
-
isatin derivatives analysis as a class of TDO inhibitors, structure-activity relationships and molecular docking studies, and optimized the inhibition potency of isatin derivatives by over 130fold, overview. Hydrogen bond interactions between the compound and key active site residues of TDO, freedom upon rotation of the C3 chemical moiety and the presence of chlorines in the benzene ring of the compound comprise the properties that an isatin-based inhibitor requires to effectively inhibit the enzymatic activity of enzyme TDO
-
additional information
identification of substituted naphthotriazolediones as tryptophan 2,3-dioxygenase (TDO) inhibitors through structure-based virtual screening, homology modeling and virtual screening, ligand docking analysis, overview
-
additional information
the enzymatic and cellular assays are influenced by many factors including detection product, reaction time and culture medium, which may cause the inconsistency of enzymatic and cellular inhibitory activities of test compounds. The TDO IC50 values of all the test compounds derived from NFK assay are 2-3 times higher than that of Kyn adduct assay
-
additional information
-
the enzymatic and cellular assays are influenced by many factors including detection product, reaction time and culture medium, which may cause the inconsistency of enzymatic and cellular inhibitory activities of test compounds. The TDO IC50 values of all the test compounds derived from NFK assay are 2-3 times higher than that of Kyn adduct assay
-
additional information
1H-indazole-4-amines inhibit both human indoleamine 2,3-dioxygenase 1 (hIDO1) and tryptophan 2,3-dioxygenase (hTDO) by a mechanism involving direct coordination with the heme ferrous and ferric states
-
additional information
-
1H-indazole-4-amines inhibit both human indoleamine 2,3-dioxygenase 1 (hIDO1) and tryptophan 2,3-dioxygenase (hTDO) by a mechanism involving direct coordination with the heme ferrous and ferric states
-
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0.0004
(1R,2S)-2-([[6-(trifluoromethyl)-1H-indazol-4-yl]amino]methyl)cyclohexan-1-ol
Homo sapiens
22°C, pH 6.5
-
0.01124
(1R,2S)-2-[[(5-bromo-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
Homo sapiens
22°C, pH 6.5
-
0.03916
(1R,2S)-2-[[(5-bromo-1H-indazol-7-yl)amino]methyl]cyclohexan-1-ol
Homo sapiens
22°C, pH 6.5
-
0.08419
(1R,2S)-2-[[(5-chloro-1H-indazol-7-yl)amino]methyl]cyclohexan-1-ol
Homo sapiens
22°C, pH 6.5
-
0.03324
(1R,2S)-2-[[(6-bromo-1-methyl-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
Homo sapiens
22°C, pH 6.5
-
0.00004
(1R,2S)-2-[[(6-bromo-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
Homo sapiens
shows efficacy against the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced mouse motor coordination deficits, comparable to Madopar, an anti-Parkinson's disease medicine, 22°C, pH 6.5
-
0.00019
(1R,2S)-2-[[(6-bromo-1H-indazol-4-yl)amino]methyl]cyclohexyl acetate
Homo sapiens
22°C, pH 6.5
-
0.00013
(1R,2S)-2-[[(6-chloro-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
Homo sapiens
22°C, pH 6.5
-
0.00041
(1R,2S)-2-[[(6-methyl-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
Homo sapiens
22°C, pH 6.5
-
0.00009
(1S,2R)-2-[[(6-bromo-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
Homo sapiens
22°C, pH 6.5
-
0.00003
(2E)-3-(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)prop-2-enoic acid
Homo sapiens
pH and temperature not specified in the publication
-
0.0044
(4-phenyl-1,2-oxazol-5-yl)methanol
Homo sapiens
pH and temperature not specified in the publication
-
0.00121
(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)boronic acid
Homo sapiens
pH and temperature not specified in the publication
-
0.000561
1-(2-methylbenzyl)-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.000768
1-(3-bromobenzyl)-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.000711
1-(3-chlorobenzyl)-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.000059
1-(3-[(4-acetyl-1-piperazinyl)carbonyl]benzyl)-1H-naphtho-[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.00003
1-(3-[(4-methyl-1-piperazinyl)carbonyl]benzyl)-1H-naphtho-[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.001586
1-(4-bromobenzyl)-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.00738
1-(4-fluorobenzyl)-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.001088
1-(4-methylbenzyl)-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.000176
1-(4-[(4-acetylpiperazin-1-yl)carbonyl]benzyl)-1H-naphtho-[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.000209
1-(4-[(4-methoxypiperidin-1-yl)carbonyl]benzyl)-1Hnaphtho[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.0135
1-(cyclopropylmethyl)-5-(1H-indol-3-yl)-1H-benzotriazole
Homo sapiens
37°C, pH 6.25
-
0.0039
1-(cyclopropylmethyl)-6-(1H-indol-3-yl)-1H-benzotriazole
Homo sapiens
37°C, pH 6.26
-
0.00015
1-cyclohexyl-2-(5H-imidazo[5,1-a]isoindol-5-yl)ethan-1-ol
Homo sapiens
22°C, pH 6.5
0.001745
1-[(3-methylphenyl)methyl]-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.00646
1-[(4-chlorophenyl)methyl]-1H-naphtho[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.00042
1-[(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)methyl]piperidine-3-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
-
0.00045
1-[(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)methyl]piperidine-4-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
-
0.00018
1-[(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)methyl]proline
Homo sapiens
pH and temperature not specified in the publication
-
0.000048
1-[3-(4-morpholinylcarbonyl)benzyl]-1H-naphtho[2,3-d]-[1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.000116
1-[4-(morpholin-4-ylcarbonyl)benzyl]-1H-naphtho[2,3-d]-[1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.000108
1-[4-[(4-methylpiperazin-1-yl)carbonyl]benzyl]-1H-naphtho-[2,3-d][1,2,3]triazole-4,9-dione
Homo sapiens
pH 8.0, 37°C
0.000145
2-(4-[(4,9-dioxo-4,9-dihydro-1H-naphtho[2,3-d][1,2,3]-triazol-1-yl)methyl]phenyl)-N,N-diethylacetamide
Homo sapiens
pH 8.0, 37°C
0.00338
2-[(6-bromo-1H-indazol-4-yl)amino]-1-(3-chlorophenyl)ethan-1-ol
Homo sapiens
22°C, pH 6.5
-
0.1477
2-[(6-bromo-1H-indazol-4-yl)amino]-1-(4-hydroxyphenyl)ethan-1-one
Homo sapiens
22°C, pH 6.5
-
0.00204
2-[(6-bromo-1H-indazol-4-yl)amino]-2-(3-chlorophenyl)ethan-1-ol
Homo sapiens
22°C, pH 6.5
-
0.00033
2-[(6-bromo-1H-indazol-4-yl)amino]-2-phenylethan-1-ol
Homo sapiens
22°C, pH 6.5
-
0.0369
2-[5-(1H-indol-3-yl)-1H-benzotriazol-1-yl]-N,N-dimethylethan-1-amine
Homo sapiens
37°C, pH 6.31
-
0.00162
2-[5-(1H-indol-3-yl)-1H-benzotriazol-1-yl]acetamide
Homo sapiens
37°C, pH 6.27
-
0.0246
2-[6-(1H-indol-3-yl)-1H-benzotriazol-1-yl]-N,N-dimethylethan-1-amine
Homo sapiens
37°C, pH 6.32
-
0.00068
2-[6-(1H-indol-3-yl)-1H-benzotriazol-1-yl]acetamide
Homo sapiens
37°C, pH 6.28
-
0.00012
2-[[(6-bromo-1H-indazol-4-yl)amino]methyl]cyclohexan-1-ol
Homo sapiens
22°C, pH 6.5
-
0.025
3-methyl-4-phenyl-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.00009
3-[(4,9-dioxo-4,9-dihydro-1H-naphtho[2,3-d][1,2,3]triazol-1-yl)methyl]-N,N-diethylbenzamide
Homo sapiens
pH 8.0, 37°C
0.000167
3-[(4,9-dioxo-4,9-dihydro-1H-naphtho[2,3-d][1,2,3]triazol-1-yl)methyl]benzoic acid
Homo sapiens
pH 8.0, 37°C
0.017
3-[5-(1H-indol-3-yl)-1H-benzotriazol-1-yl]propane-1,2-diol
Homo sapiens
37°C, pH 6.46
-
0.0252
3-[6-(1H-indol-3-yl)-1H-benzotriazol-1-yl]propane-1,2-diol
Homo sapiens
37°C, pH 6.47
-
0.00029
4-(1H-pyrazol-1-yl)-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.0005
4-(3-chlorophenyl)-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.00033
4-(3-chlorophenyl)-imidazole
Homo sapiens
pH and temperature not specified in the publication
-
0.0031
4-(3-methoxyphenyl)-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.0016
4-(3-methyl-1H-pyrazol-1-yl)-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.00083
4-(4-chlorophenyl)-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.00034
4-(4-fluoro-1H-pyrazol-1-yl)-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.00058
4-(4-fluorophenyl)-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.0016
4-(4-methyl-1H-pyrazol-1-yl)-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.0017
4-(pyridin-2-yl)-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.0023
4-(pyridin-3-yl)-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.000029
4-(thiophen-2-yl)-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.000028
4-(thiophen-3-yl)-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.02702
4-([[(1S,2R)-2-hydroxycyclohexyl]methyl]amino)-1H-indazole-6-carboxylic acid
Homo sapiens
22°C, pH 6.5
-
0.00011
4-chlorophenyl-1,2,3-triazol-4-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.0078
4-cyclohexyl-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.00064
4-cyclopentyl-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.00014
4-phenyl-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.018
4-phenyl-1,2-thiazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.00048
4-phenylimidazole
Homo sapiens
pH and temperature not specified in the publication
0.01286
4-[(1Z)-2-[(6-bromo-1H-indazol-4-yl)amino]-N-hydroxyethanimidoyl]phenol
Homo sapiens
22°C, pH 6.5
-
0.000181
4-[(4,9-dioxo-4,9-dihydro-1H-naphtho[2,3-d][1,2,3]triazol-1-yl)methyl]-N,N-diethylbenzamide
Homo sapiens
pH 8.0, 37°C
0.000312
4-[(4,9-dioxo-4,9-dihydro-1H-naphtho[2,3-d][1,2,3]triazol-1-yl)methyl]benzoic acid
Homo sapiens
pH 8.0, 37°C
0.00185
4-[[(6-bromo-1H-indazol-4-yl)amino]methyl]phenol
Homo sapiens
22°C, pH 6.5
-
0.015
5-(1H-indol-3-yl)-1-(2,2,2-trifluoroethyl)-1H-benzotriazole
Homo sapiens
37°C, pH 6.23
-
0.00501
5-(1H-indol-3-yl)-1-methyl-1H-benzotriazol-4-amine
Homo sapiens
37°C, pH 6.17
-
0.00387
5-(1H-indol-3-yl)-1-methyl-1H-benzotriazole
Homo sapiens
37°C, pH 6.13
-
0.0369
5-(1H-indol-3-yl)-1-[(oxolan-2-yl)methyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.35
-
0.0441
5-(1H-indol-3-yl)-1-[(oxolan-3-yl)methyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.33
-
0.01773
5-(1H-indol-3-yl)-1-[(piperidin-4-yl)methyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.39
-
0.1186
5-(1H-indol-3-yl)-1-[2-(morpholin-4-yl)ethyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.37
-
0.0249
5-(1H-indol-3-yl)-1-[2-(piperazin-1-yl)ethyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.43
-
0.0261
5-(1H-indol-3-yl)-1-[2-(pyrrolidin-3-yl)ethyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.41
-
0.00385
5-(1H-indol-3-yl)-2-methyl-2H-benzotriazol-4-amine
Homo sapiens
37°C, pH 6.16
-
0.004
5-(1H-indol-3-yl)-2-methyl-2H-benzotriazole
Homo sapiens
37°C, pH 6.12
-
0.0011
5-(6-fluoro-1H-indol-3-yl)-1-methyl-1H-benzotriazole
Homo sapiens
37°C, pH 6.14
-
0.045
5-(6-fluoro-1H-indol-3-yl)-1-[2-(piperazin-1-yl)ethyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.44
-
0.0019
6-(1H-indol-3-yl)-1-(2,2,2-trifluoroethyl)-1H-benzotriazole
Homo sapiens
37°C, pH 6.24
-
0.00393
6-(1H-indol-3-yl)-1-methyl-1H-benzotriazol-7-amine
Homo sapiens
37°C, pH 6.18
-
0.00908
6-(1H-indol-3-yl)-1-methyl-1H-[1,2,3]triazolo[4,5-b]pyridine
Homo sapiens
37°C, pH 6.21
-
0.00132
6-(1H-indol-3-yl)-1-methyl-7-nitro-1H-benzotriazole
Homo sapiens
37°C, pH 6.22
-
0.0211
6-(1H-indol-3-yl)-1-[(oxolan-2-yl)methyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.36
-
0.0219
6-(1H-indol-3-yl)-1-[(oxolan-3-yl)methyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.34
-
0.02551
6-(1H-indol-3-yl)-1-[(piperidin-4-yl)methyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.40
-
0.04565
6-(1H-indol-3-yl)-1-[(pyrrolidin-3-yl)methyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.42
-
0.0526
6-(1H-indol-3-yl)-1-[2-(morpholin-4-yl)ethyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.38
-
0.0052
6-(1H-indol-3-yl)-1-[2-(piperazin-1-yl)ethyl]-1H-benzotriazole
Homo sapiens
37°C, pH 6.45
-
0.002 - 0.00602
6-(1H-indol-3-yl)-1H-benzotriazole
-
0.01306
6-(1H-indol-3-yl)-2-methyl-2H-[1,2,3]triazolo[4,5-b]pyridine
Homo sapiens
37°C, pH 6.19
-
0.00783
6-(1H-indol-3-yl)-3-methyl-3H-[1,2,3]triazolo[4,5-b]pyridine
Homo sapiens
37°C, pH 6.20
-
0.0049 - 0.0066
6-(1H-indol-3-yl)isoquinoline
Homo sapiens
37°C, pH 6.7
-
0.0128 - 0.0169
6-(1H-indol-3-yl)quinazoline
Homo sapiens
37°C, pH 6.8
-
0.0017
6-bromo-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.00086
6-bromo-N-(cyclohexylmethyl)-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.00204
6-bromo-N-[(1,4-dioxaspiro[4.5]decan-6-yl)methyl]-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.05841
6-bromo-N-[(1R,2R)-2-hydroxycyclohexyl]-1H-indazole-4-carboxamide
Homo sapiens
22°C, pH 6.5
-
0.00311
6-bromo-N-[(pyridin-2-yl)methyl]-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.01044
6-bromo-N-[(pyrrolidin-3-yl)methyl]-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.00022
6-bromo-N-[[(1S,2S)-2-chlorocyclohexyl]methyl]-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.00185
6-bromo-N-[[(2R)-piperidin-2-yl]methyl]-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.00745
6-bromo-N-[[(2R)-pyrrolidin-2-yl]methyl]-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.00606
6-bromo-N-[[(2S)-piperidin-2-yl]methyl]-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.00417
6-bromo-N-[[(2S)-pyrrolidin-2-yl]methyl]-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.0061 - 0.0087
6-fluoro-3-[(E)-2-(1H-tetrazol-5-yl)ethenyl]-1H-indole
Homo sapiens
37°C, pH 6.5
-
0.0127 - 0.0229
7-(1H-indol-3-yl)-3,4-dihydroquinazolin-2(1H)-one
Homo sapiens
37°C, pH 6.10
-
0.0056 - 0.0071
7-(1H-indol-3-yl)isoquinoline
Homo sapiens
37°C, pH 6.6
-
0.0212 - 0.0326
7-(1H-indol-3-yl)quinazoline
Homo sapiens
37°C, pH 6.9
-
0.00602
8-fluoro-2-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)indolo[2,1-b]quinazoline-6,12-dione
Homo sapiens
pH and temperature not specified in the publication
-
0.00113
8-fluoro-2-[(1H-1,2,3-triazol-1-yl)methyl]indolo[2,1-b]quinazoline-6,12-dione
Homo sapiens
pH and temperature not specified in the publication
-
0.00006
8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazoline-2-carbaldehyde
Homo sapiens
pH and temperature not specified in the publication
-
0.00037
ethyl (2E)-3-(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)prop-2-enoate
Homo sapiens
pH and temperature not specified in the publication
-
0.00287
methyl 1-[(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)methyl]piperidine-3-carboxylate
Homo sapiens
pH and temperature not specified in the publication
-
0.00099
methyl 1-[(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)methyl]piperidine-4-carboxylate
Homo sapiens
pH and temperature not specified in the publication
-
0.0003
methyl 1-[(8-fluoro-6,12-dioxo-6,12-dihydroindolo[2,1-b]quinazolin-2-yl)methyl]prolinate
Homo sapiens
pH and temperature not specified in the publication
-
0.01259
methyl 4-([[(1S,2R)-2-hydroxycyclohexyl]methyl]amino)-1H-indazole-6-carboxylate
Homo sapiens
22°C, pH 6.5
-
0.00777
N-(3-bromo-4-fluorophenyl)-N'-hydroxy-4-[[2-(sulfamoylamino)ethyl]amino]-1,2,5-oxadiazole-3-carboximidamide
Homo sapiens
22°C, pH 6.5
-
0.00045
N-(4-[[(6-bromo-1H-indazol-4-yl)amino]methyl]cyclohexylidene)hydroxylamine
Homo sapiens
22°C, pH 6.5
-
0.00019
N-methyl-4-phenyl-1,2-oxazol-5-amine
Homo sapiens
pH and temperature not specified in the publication
-
0.04487
N-[(azetidin-3-yl)methyl]-6-bromo-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.00036
N-[[(1S,2R)-2-aminocyclohexyl]methyl]-6-bromo-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.00091
N-[[(1S,2S)-2-aminocyclohexyl]methyl]-6-bromo-1H-indazol-4-amine
Homo sapiens
22°C, pH 6.5
-
0.00136
tert-butyl 3-[[(6-bromo-1H-indazol-4-yl)amino]methyl]pyrrolidine-1-carboxylate
Homo sapiens
22°C, pH 6.5
-
0.1738
[5-(1H-indol-3-yl)-1H-benzotriazol-1-yl]acetic acid
Homo sapiens
37°C, pH 6.29
-
0.1045
[6-(1H-indol-3-yl)-1H-benzotriazol-1-yl]acetic acid
Homo sapiens
37°C, pH 6.30
-
additional information
additional information
-
0.002 - 0.0034
6-(1H-indol-3-yl)-1H-benzotriazole
Homo sapiens
37°C, pH 6.11
-
0.00602
6-(1H-indol-3-yl)-1H-benzotriazole
Homo sapiens
37°C, pH 6.15
-
additional information
additional information
Homo sapiens
the enzymatic and cellular assays are influenced by many factors including detection product, reaction time and culture medium, which may cause the inconsistency of enzymatic and cellular inhibitory activities of test compounds. The IC50 values of all the test compounds derived from NFK assay are 2-3 times higher than that of Kyn adduct assay
-
additional information
additional information
Homo sapiens
-
the enzymatic and cellular assays are influenced by many factors including detection product, reaction time and culture medium, which may cause the inconsistency of enzymatic and cellular inhibitory activities of test compounds. The IC50 values of all the test compounds derived from NFK assay are 2-3 times higher than that of Kyn adduct assay
-
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drug target
conversion of tryptophan to N-formylkynurenine is the first and rate-limiting step of the tryptophan metabolic pathway (i.e., the kynurenine pathway). This conversion is catalyzed by three enzyme isoforms: indoleamine 2,3-dioxygenase 1 (IDO1), indoleamine 2,3-dioxygenase 2 (IDO2), and tryptophan-2,3-dioxygenase (TDO). As this pathway generates numerous metabolites that are involved in various pathological conditions, IDOs and TDO represent important targets for therapeutic intervention. Despite their poor sequence similarities, their active sites are highly conserved, and therefore allow the design of inhibitors with multiple activities that can target at least two isoforms
drug target
human indoleamine 2,3-dioxygenase 1 (hIDO1) and tryptophan 2,3-dioxygenase (hTDO) are closely linked to the pathogenesis of Parkinson's disease
drug target
Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO) are promising drug development targets due to their implications in pathologies such as cancer and neurodegenerative diseases. IDO1/TDO dual inhibitors and provides chemical molecules for potential development into drugs
drug target
the enzyme (TDO2) catalyzes the conversion of tryptophan to the immunosuppressive metabolite kynurenine. TDO2 overexpression has been observed in a number of cancers. Therefore, TDO inhibition may be a useful therapeutic intervention for cancers
drug target
tryptophan 2,3-dioxygenase is a therapeutic target for Parkinson's disease
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes that catalyze the O2-dependent oxidation of L-tryptophan (L-Trp) in biological systems following different reaction mechanisms, the rate-limiting step in the IDO and TDO mechanisms is not the same
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes that catalyze the O2-dependent oxidation of L-tryptophan (L-Trp) in biological systems following different reaction mechanisms, the rate-limiting step in the IDO and TDO mechanisms is not the same
evolution
-
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
evolution
-
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes that catalyze the O2-dependent oxidation of L-tryptophan (L-Trp) in biological systems following different reaction mechanisms, the rate-limiting step in the IDO and TDO mechanisms is not the same
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malfunction
TDO knockout mice require a minimum of 0.06% dietary L-Trp, which value is about 2 mg/d/mouse
malfunction
alterations in the activity of tryptophan 2,3-dioxygenase cause imbalances in the levels of serotonin and other neuroactive metabolites which can contribute to motor, psychiatric, gastrointestinal, and other dysfunctions often seen in Parkinson's disease
malfunction
pharmacological inhibition or knockdown of the enzyme (TDO2) in adjuvant-induced arthritis-fibroblast-like synoviocytes results in a reduced proliferation, secretion, migration and invasion
malfunction
pharmacological inhibition or knockdown of the enzyme (TDO2) in adjuvant-induced arthritis-fibroblast-like synoviocytes results in a reduced proliferation, secretion, migration and invasion
malfunction
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TDO knockout mice require a minimum of 0.06% dietary L-Trp, which value is about 2 mg/d/mouse
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metabolism
comparison of contribution percentage of tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) to the conversion of L-tryptophan, the calculated percentage conversions indicats that TDO and IDO oxidize 70% and 30%, respectively, of the dietary L-tryptophan. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low, this amount of D-Trp is converted to L-Trp, which is primarily used for protein synthesis rather than catabolism via the Kyn biosynthesis pathway in mice
metabolism
the first and rate limiting step of the kynurenine pathway is carried out by two heme-containing enzymes, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52), which differ in their tissue distribution and regulation
metabolism
weaning alters the tryptophan 2,3-dioxygenase activity by affecting the acetylation state of the enzyme in piglets livers
metabolism
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comparison of contribution percentage of tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) to the conversion of L-tryptophan, the calculated percentage conversions indicats that TDO and IDO oxidize 70% and 30%, respectively, of the dietary L-tryptophan. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low, this amount of D-Trp is converted to L-Trp, which is primarily used for protein synthesis rather than catabolism via the Kyn biosynthesis pathway in mice
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physiological function
the enzyme is involved in L-tryptophan catabolism to produce bioactive metabolites including kynurenine, kynurenic acid, quinolinic acid, and the coenzyme NAD+ via the kynurenine pathway
physiological function
the enzyme is involved in nicotinamide biosynthesis. Comparison of contribution percentage of tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) to the conversion of L-tryptophan, the calculated percentage conversions indicats that TDO and IDO oxidize 70% and 30%, respectively, of the dietary L-tryptophan. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low, this amount of D-Trp is converted to L-Trp, which is primarily used for protein synthesis rather than catabolism via the Kyn biosynthesis pathway in mice
physiological function
the human heme enzyme tryptophan 2,3-dioxygenase (hTDO) catalyzes the insertion of dioxygen into its cognate substrate, L-tryptophan (L-Trp)
physiological function
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tryptophan 2,3-dioxygenase (TDO) has a immunomodulatory function that promotes tumoral immune resistance and proliferation
physiological function
tryptophan 2,3-dioxygenase (TDO) is one of the two key enzymes in the kynurenine pathway, it catalyzes the indole ring cleavage at the C2-C3 bond of L-tryptophan. This is a rate-limiting step in the regulation of tryptophan concentration in vivo. In addition to its role in protein synthesis, 95% of L-Trp in the human body is processed by the kynurenine pathway, leading to the production of nicotinamide adenine dinucleotide. Enzyme TDO is expressed in many tumor cells and is related to reduction of antitumor immune response
physiological function
conversion of tryptophan to N-formylkynurenine is the first and rate-limiting step of the tryptophan metabolic pathway (i.e., the kynurenine pathway). This conversion is catalyzed by three enzyme isoforms: indoleamine 2,3-dioxygenase 1 (IDO1), indoleamine 2,3-dioxygenase 2 (IDO2), and tryptophan-2,3-dioxygenase (TDO)
physiological function
rate limiting enzyme of tryptophan metabolism
physiological function
TDO2 is the key enzyme responsible for reduced tryptophan levels in mut-MED12 leiomyoma
physiological function
the enzyme (TDO2) catalyzes the conversion of tryptophan to the immunosuppressive metabolite kynurenine
physiological function
the enzyme catalyses the rate-limiting step in the kynurenine pathway, an important biochemical mechanism for immunological responsecancers express tryptophan catabolising enzymes indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO2) to produce immunosuppressive tryptophan metabolites that undermine thr immune systems of patients, leading to poor disease outcomes
physiological function
the enzyme is overactivated or overexpressed in many human cancers, which is associated with poor patient outcomes
physiological function
the enzyme is responsible for L-tryptophan (L-Trp) homeostasis. Expression of TDO2 in cancer cells results in the inhibition of immune-mediated tumor rejection due to an enhancement of L-Trp catabolism via the kynurenine pathway
physiological function
the enzyme plays a key role in regulating the activation of fibroblast-like synoviocytes in autoimmune arthritis
physiological function
the enzyme plays a key role in regulating the activation of fibroblast-like synoviocytes in autoimmune arthritis
physiological function
the first step of the kynurenine pathway for L-tryptophan (L-Trp) degradation is catalyzed by heme-dependent dioxygenases, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase
physiological function
-
the kynurenine pathway is the major route of tryptophan metabolism. The first step of this pathway is catalysed by one of two heme-dependent dioxygenase enzymes - tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) - leading initially to the formation of N-formylkynurenine
physiological function
tryptophan 2,3-dioxygenase catalyzes the oxidation of the essential amino acid tryptophan to N-formylkynurenine which is rapidly converted to a series of biological active metabolites including kynurenine via the kynurenine pathway
physiological function
tryptophan 2,3-dioxygenase is a key enzyme of tryptophan metabolism at the entry of the kynurenine pathway which moderates production of neuroactive compounds primarily outside the central nervous system
physiological function
tryptophan 2,3-dioxygenase is the rate-limiting enzyme in the kynurenine pathway. It catalyzes the oxidative breakdown of the essential amino acid, L-tryptophan to N-formylkynurenine. This reaction is also carried out by an analogous hemoprotein, indoleamine 2,3-dioxygenase, albeit with a much lower substrate selectivity
physiological function
tryptophanemia is controlled by a tryptophan-sensing mechanism ubiquitinating tryptophan 2,3-dioxygenase. A mechanism allows stable tryptophanemia despite varying levels of tryptophan supply in the diet. High tryptophan availability stabilizes tryptophan 2,3-dioxygenase in the liver, allowing efficient tryptophan catabolism. In contrast, low tryptophan levels trigger proteasome-mediated degradation of tryptophan 2,3-dioxygenase, thereby stopping tryptophan catabolism and preventing hypotryptophanemia
physiological function
-
the enzyme is involved in nicotinamide biosynthesis. Comparison of contribution percentage of tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) to the conversion of L-tryptophan, the calculated percentage conversions indicats that TDO and IDO oxidize 70% and 30%, respectively, of the dietary L-tryptophan. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low, this amount of D-Trp is converted to L-Trp, which is primarily used for protein synthesis rather than catabolism via the Kyn biosynthesis pathway in mice
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physiological function
-
the first step of the kynurenine pathway for L-tryptophan (L-Trp) degradation is catalyzed by heme-dependent dioxygenases, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase
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additional information
eight residues play critical roles in L-tryptophan oxidation, i.e. Y42, Y45, F72, H76, F140, R144, S151, and H328. hTDO must form an oligomer to exhibit activity
additional information
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eight residues play critical roles in L-tryptophan oxidation, i.e. Y42, Y45, F72, H76, F140, R144, S151, and H328. hTDO must form an oligomer to exhibit activity
additional information
no evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
additional information
no evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
additional information
TDO homology modeling, overview
additional information
the active site of the enzyme is highly dynamic
additional information
-
the active site of the enzyme is highly dynamic
additional information
the exo site regulates hTDO cellular stability
additional information
-
the exo site regulates hTDO cellular stability
additional information
-
no evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
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Basran, J.; Booth, E.S.; Lee, M.; Handa, S.; Raven, E.L.
Analysis of reaction intermediates in tryptophan 2,3-dioxygenase a comparison with indoleamine 2,3-dioxygenase
Biochemistry
55
6743-6750
2016
Homo sapiens (P48775), Xanthomonas campestris pv. campestris (Q8PDA8), Xanthomonas campestris pv. campestris ATCC 33913 (Q8PDA8)
brenda
Maeta, A.; Sano, M.; Fukuwatari, T.; Funakoshi, H.; Nakamura, T.; Shibata, K.
Contributions of tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase to the conversion of D-tryptophan to nicotinamide analyzed by using tryptophan 2,3-dioxygenase-knockout mice
Biosci. Biotechnol. Biochem.
78
878-881
2014
Mus musculus (P48776), Mus musculus C57BL/6 (P48776)
brenda
Pantouris, G.; Loudon-Griffiths, J.; Mowat, C.G.
Insights into the mechanism of inhibition of tryptophan 2,3-dioxygenase by isatin derivatives
J. Enzyme Inhib. Med. Chem.
31
70-78
2016
Homo sapiens
brenda
Yuasa, H.J.; Ball, H.J.
Efficient tryptophan-catabolizing activity is consistently conserved through evolution of TDO enzymes, but not IDO enzymes
J. Exp. Zool. B
324
128-140
2015
no activity in Saccharomyces cerevisiae, no activity in Schistosoma mansoni, Strongylocentrotus purpuratus, no activity in Brugia malayi, Nematostella vectensis (A7RFF0), Monosiga brevicollis (A9V766), Branchiostoma floridae (C3XXE6), Drosophila melanogaster (P20351), Rattus norvegicus (P21643), Homo sapiens (P48775), Caenorhabditis elegans (Q09474)
brenda
Wu, J.S.; Lin, S.Y.; Liao, F.Y.; Hsiao, W.C.; Lee, L.C.; Peng, Y.H.; Hsieh, C.L.; Wu, M.H.; Song, J.S.; Yueh, A.; Chen, C.H.; Yeh, S.H.; Liu, C.Y.; Lin, S.Y.; Yeh, T.K.; Hsu, J.T.; Shih, C.; Ueng, S.H.; Hung, M.S.; Wu, S.Y.
Identification of substituted naphthotriazolediones as novel tryptophan 2,3-dioxygenase (TDO) inhibitors through structure-based virtual screening
J. Med. Chem.
58
7807-7819
2015
Homo sapiens (P48775)
brenda
Nienhaus, K.; Hahn, V.; Huepfel, M.; Nienhaus, G.U.
Substrate binding primes human tryptophan 2,3-dioxygenase for ligand binding
J. Phys. Chem. B
121
7412-7420
2017
Homo sapiens (P48775), Homo sapiens
brenda
Gonzalez Esquivel, D.; Ramirez-Ortega, D.; Pineda, B.; Castro, N.; Rios, C.; Perez de la Cruz, V.
Kynurenine pathway metabolites and enzymes involved in redox reactions
Neuropharmacology
112
331-345
2017
Homo sapiens (P14902), Homo sapiens (P48775), Homo sapiens (Q6ZQW0), Mus musculus (P28776), Xanthomonas campestris pv. campestris (Q8PDA8), Xanthomonas campestris pv. campestris ATCC 33913 (Q8PDA8)
brenda
Meng, B.; Wu, D.; Gu, J.; Ouyang, S.; Ding, W.; Liu, Z.
Structural and functional analyses of human tryptophan 2,3-dioxygenase
Proteins
82
3210-3216
2014
Homo sapiens (P48775), Homo sapiens
brenda
Lewis-Ballester, A.; Forouhar, F.; Kim, S.M.; Lew, S.; Wang, Y.; Karkashon, S.; Seetharaman, J.; Batabyal, D.; Chiang, B.Y.; Hussain, M.; Correia, M.A.; Yeh, S.R.; Tong, L.
Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase
Sci. Rep.
6
35169
2016
Homo sapiens (P48775), Homo sapiens
brenda
Pei, Z.; Mendonca, R.; Gazzard, L.; Pastor, R.; Goon, L.; Gustafson, A.; VanderPorten, E.; Hatzivassiliou, G.; Dement, K.; Cass, R.; Yuen, P.W.; Zhang, Y.; Wu, G.; Lin, X.; Liu, Y.; Sellers, B.D.
Aminoisoxazoles as potent inhibitors of tryptophan 2,3-dioxygenase 2 (TDO2)
ACS Med. Chem. Lett.
9
417-421
2018
Homo sapiens (P48775), Homo sapiens
brenda
Wei, Y.; Lu, C.; Jiang, S.; Zhang, Y.; Li, Q.; Bai, W.J.; Wang, X.
Directed evolution of a tryptophan 2,3-dioxygenase for the diastereoselective monooxygenation of tryptophans
Angew. Chem. Int. Ed. Engl.
59
3043-3047
2020
Xanthomonas campestris
brenda
Liu, Y.; Kim, S.M.; Wang, Y.; Karkashon, S.; Lewis-Ballester, A.; Yeh, S.R.; Correia, M.A.
Characterization of the structural determinants of the ubiquitin-dependent proteasomal degradation of human hepatic tryptophan 2,3-dioxygenase
Biochem. J.
478
1999-2017
2021
Homo sapiens (P48775), Homo sapiens
brenda
Geng, J.; Weitz, A.C.; Dornevil, K.; Hendrich, M.P.; Liu, A.
Kinetic and spectroscopic characterization of the catalytic ternary complex of tryptophan 2,3-dioxygenase
Biochemistry
59
2813-2822
2020
Cupriavidus metallidurans (Q1LK00), Cupriavidus metallidurans, Cupriavidus metallidurans ATCC 43123 (Q1LK00)
brenda
Zhang, S.; Guo, L.; Yang, D.; Xing, Z.; Li, W.; Kuang, C.; Yang, Q.
Evaluation and comparison of the commonly used bioassays of human indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO)
Bioorg. Chem.
104
104348
2020
Homo sapiens (P48775), Homo sapiens
brenda
Li, Y.; Zhang, S.; Wang, R.; Cui, M.; Liu, W.; Yang, Q.; Kuang, C.
Synthesis of novel tryptanthrin derivatives as dual inhibitors of indoleamine 2,3-dioxygenase 1 and tryptophan 2,3-dioxygenase
Bioorg. Med. Chem. Lett.
30
127159
2020
Homo sapiens (P48775)
brenda
Chang, Y.; Han, P.; Wang, Y.; Jia, C.; Zhang, B.; Zhao, Y.; Li, S.; Li, S.; Wang, X.; Yang, X.; Wei, W.
Tryptophan 2,3-dioxygenase 2 plays a key role in regulating the activation of fibroblast-like synoviocytes in autoimmune arthritis
Br. J. Pharmacol.
179
3024-3042
2022
Rattus norvegicus (P21643), Homo sapiens (P48775)
brenda
Boros, F.A.; Vecsei, L.
Tryptophan 2,3-dioxygenase, a novel therapeutic target for Parkinsons disease
Expert Opin. Ther. Targets
25
877-888
2021
Homo sapiens (P48775)
brenda
Basran, J.; Booth, E.S.; Campbell, L.P.; Thackray, S.J.; Jesani, M.H.; Clayden, J.; Moody, P.C.E.; Mowat, C.G.; Kwon, H.; Raven, E.L.
Binding of L-kynurenine to X. campestris tryptophan 2,3-dioxygenase
J. Inorg. Biochem.
225
111604
2021
Xanthomonas campestris, Xanthomonas campestris pv. campestris (Q8PDA8), Xanthomonas campestris pv. campestris ATCC 33913 (Q8PDA8)
brenda
Kozlova, A.; Thabault, L.; Liberelle, M.; Klaessens, S.; Prevost, J.R.C.; Mathieu, C.; Pilotte, L.; Stroobant, V.; Van den Eynde, B.; Frederick, R.
Rational design of original fused-cycle selective inhibitors of tryptophan 2,3-dioxygenase
J. Med. Chem.
64
10967-10980
2021
Homo sapiens (P48775)
brenda
Ning, X.L.; Li, Y.Z.; Huo, C.; Deng, J.; Gao, C.; Zhu, K.R.; Wang, M.; Wu, Y.X.; Yu, J.L.; Ren, Y.L.; Luo, Z.Y.; Li, G.; Chen, Y.; Wang, S.Y.; Peng, C.; Yang, L.L.; Wang, Z.Y.; Wu, Y.; Qian, S.; Li, G.B.
X-ray structure-guided discovery of a potent, orally bioavailable, dual human indoleamine/tryptophan 2,3-dioxygenase (hIDO/hTDO) inhibitor that shows activity in a mouse model of Parkinsons disease
J. Med. Chem.
64
8303-8332
2021
Homo sapiens (P48775), Homo sapiens
brenda
Huang, L.; Yao, W.; Wang, T.; Li, J.; He, Q.; Huang, F.
Acetylation of phenylalanine hydroxylase and tryptophan 2,3-dioxygenase alters hepatic aromatic amino acid metabolism in weaned piglets
Metabolites
10
146
2020
Sus scrofa (F1RWA8)
brenda
Sari, S.; Tomek, P.; Leung, E.; Reynisson, J.
Discovery and characterisation of dual inhibitors of tryptophan 2,3-dioxygenase (TDO2) and indoleamine 2,3-dioxygenase 1 (IDO1) using virtual screening
Molecules
24
4346
2019
Homo sapiens (P48775), Homo sapiens
brenda
Dolsak, A.; Gobec, S.; Sova, M.
Indoleamine and tryptophan 2,3-dioxygenases as important future therapeutic targets
Pharmacol. Ther.
221
107746
2021
Homo sapiens, Homo sapiens (P14902), Homo sapiens (Q6ZQW0)
brenda
Klaessens, S.; Stroobant, V.; Hoffmann, D.; Gyrd-Hansen, M.; Pilotte, L.; Vigneron, N.; De Plaen, E.; Van den Eynde, B.J.
Tryptophanemia is controlled by a tryptophan-sensing mechanism ubiquitinating tryptophan 2,3-dioxygenase
Proc. Natl. Acad. Sci. USA
118
e2022447118
2021
Homo sapiens (P48775)
brenda
Hutchinson, A.P.; Yin, P.; Neale, I.; Coon, J.S.; Kujawa, S.A.; Liu, S.; Bulun, S.E.
Tryptophan 2,3-dioxygenase-2 in uterine Leiomyoma dysregulation by MED12 mutation status
Reprod. Sci.
29
743-749
2022
Homo sapiens (P48775)
brenda