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0.66 - 0.747
1-methyl-D-tryptophan
0.062 - 0.696
1-methyl-L-tryptophan
0.006 - 100
5-fluoro-DL-tryptophan
0.006 - 0.36
5-fluoro-tryptophan
0.6
5-hydroxy-D-tryptophan
-
24°C
0.017 - 0.68
5-hydroxy-L-tryptophan
0.017
5-hydroxy-tryptophan
-
0.113 - 0.547
5-methoxy-DL-tryptophan
0.088 - 1.57
5-methyl-DL-tryptophan
0.098
5-methyl-tryptophan
-
0.186 - 186
6-fluoro-DL-tryptophan
0.056 - 3.457
6-methyl-DL-tryptophan
0.00072 - 62.4
L-tryptophan
additional information
additional information
-
0.66
1-methyl-D-tryptophan
pH 6.5, 25°C, recombinant enzyme IDO1
0.747
1-methyl-D-tryptophan
pH 7.5, 25°C, recombinant enzyme IDO2
0.062
1-methyl-L-tryptophan
-
-
0.07
1-methyl-L-tryptophan
pH 6.5, 25°C, recombinant enzyme IDO1
0.696
1-methyl-L-tryptophan
pH 7.5, 25°C, recombinant enzyme IDO2
0.006
5-fluoro-DL-tryptophan
pH 6.5, 25°C, recombinant enzyme IDO1
0.1
5-fluoro-DL-tryptophan
O2 not present at a saturating level
0.183
5-fluoro-DL-tryptophan
H55S mutant enzyme, O2 not present at a saturating level
0.194
5-fluoro-DL-tryptophan
H55A mutant enzyme, O2 not present at a saturating level
1.768
5-fluoro-DL-tryptophan
pH 7.5, 25°C, recombinant enzyme IDO2
100
5-fluoro-DL-tryptophan
25°C, pH 7.5, wild-type enzyme
0.006
5-fluoro-tryptophan
-
0.36
5-fluoro-tryptophan
-
0.017
5-hydroxy-L-tryptophan
pH 6.5, 25°C, recombinant enzyme IDO1
0.02
5-hydroxy-L-tryptophan
-
24°C
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, 37°C, 10-60 min
0.1
5-hydroxy-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, 37°C, 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, 37°C, 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, 37°C, 10-60 min
0.21
5-hydroxy-L-tryptophan
-
37°C, 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, 37°C, 10-60 min
0.44
5-hydroxy-L-tryptophan
-
-
0.44
5-hydroxy-L-tryptophan
-
recombinant enzyme
0.68
5-hydroxy-L-tryptophan
37°C, pH 6.5
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, 37°C, 10 min
0.547
5-methoxy-DL-tryptophan
pH 7.5, 25°C, recombinant enzyme IDO2
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, 37°C, 10 min
0.098
5-methyl-DL-tryptophan
pH 6.5, 25°C, recombinant enzyme IDO1
0.357
5-methyl-DL-tryptophan
O2 not present at a saturating level
0.395
5-methyl-DL-tryptophan
H55A mutant enzyme, O2 not present at a saturating level
1.302
5-methyl-DL-tryptophan
H55S mutant enzyme
1.57
5-methyl-DL-tryptophan
pH 7.5, 25°C, recombinant enzyme IDO2
0.186
6-fluoro-DL-tryptophan
O2 not present at a saturating level
0.195
6-fluoro-DL-tryptophan
H55A mutant enzyme, O2 not present at a saturating level
0.546
6-fluoro-DL-tryptophan
H55S mutant enzyme, O2 not present at a saturating level
186
6-fluoro-DL-tryptophan
25°C, pH 7.5, wild-type enzyme
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, 37°C, 10 min
0.386
6-methyl-DL-tryptophan
H55A mutant enzyme, O2 not present at a saturating level
0.975
6-methyl-DL-tryptophan
O2 not present at a saturating level
1.98
6-methyl-DL-tryptophan
H55S mutant enzyme, O2 not present at a saturating level
3.457
6-methyl-DL-tryptophan
pH 7.5, 25°C, recombinant enzyme IDO2
0.3
D-Trp
-
-
5
D-Trp
-
recombinant enzyme
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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 10-60 min
0.062
D-tryptophan
-
pH 7.5, 37 °C, 40 min incubation time
0.159
D-tryptophan
-
pH 7.0, 25°C, mutant T342A
0.18
D-tryptophan
-
pH 7.0
0.26
D-tryptophan
-
pH 7.0, 25°C, wild-type enzyme
0.296
D-tryptophan
pH 6.5, 25°C, recombinant enzyme IDO1
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, 25°C
1.3
D-tryptophan
-
pH 7.0, 1 mM 3-indoleethanol
1.7
D-tryptophan
-
pH 7.0
2.6
D-tryptophan
pH and temperature not specified in the publication
3.609
D-tryptophan
pH 7.5, 25°C, recombinant enzyme IDO2
3.795
D-tryptophan
-
50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37°C, 10 min
5.2
D-tryptophan
37°C, pH 6.5
7.3
D-tryptophan
-
37°C, pH 6.5
16
D-tryptophan
pH and temperature not specified in the publication
0.02
L-Trp
-
-
0.02
L-Trp
-
recombinant enzyme
0.114
L-Trp
25°C, pH 7.5, wild-type enzyme
7.7
L-Trp
-
activated by 0.033 mM Cd2+
133
L-Trp
25°C, pH 7.5, mutant enzyme H55A
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 37°C
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 37°C
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 37°C
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 37°C
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 37°C
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 37°C
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 37°C
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 37°C
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, 37°C, 10-60 min
0.0065
L-tryptophan
-
pH 8.0
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, 37°C, 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, 37°C, 10-60 min
0.01
L-tryptophan
-
pH 7.5, 37 °C, 5 min incubation time
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 37°C
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 37°C
0.013
L-tryptophan
-
pH 7.0
0.0141
L-tryptophan
pH 7.0, 22°C, 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, 37°C, 10 min
0.0191
L-tryptophan
pH 6.5, 37°C
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, 37°C, 10-60 min
0.02
L-tryptophan
pH and temperature not specified in the publication
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, 37°C, 10-60 min
0.0209
L-tryptophan
pH 6.5, 25°C, recombinant enzyme IDO1
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 37°C
0.023
L-tryptophan
recombinant wild-type enzyme, pH 7.4, 25°C
0.0234
L-tryptophan
A4T mutant protein
0.025
L-tryptophan
-
pH 6.5
0.026
L-tryptophan
-
37°C, 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 37°C
0.028
L-tryptophan
-
recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C
0.028
L-tryptophan
-
IDO1, pH and temperature not specified in the publication, MB assay
0.029
L-tryptophan
-
recombinant isozyme IDO1, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C
0.029
L-tryptophan
-
IDO1, pH and temperature not specified in the publication, cytochrome b5 assay
0.0296
L-tryptophan
R77H mutant protein
0.0342
L-tryptophan
R77K mutant protein
0.05
L-tryptophan
-
pH 6.0
0.0526
L-tryptophan
pH 6.5, 37°C, recombinant His-tagged enzyme
0.074
L-tryptophan
pH 6.5, 37°C
0.074
L-tryptophan
37°C, pH 6.5
0.0745
L-tryptophan
pH 6.5, 37°C, recombinant His-tagged enzyme in presence of inhibitor galanal
0.0825
L-tryptophan
-
pH 8.0, normal atmospheric conditions
0.112
L-tryptophan
recombinant mutant T379A, pH 7.4, 25°C
0.114
L-tryptophan
O2 not present at a saturating level
0.114
L-tryptophan
pH and temperature not specified in the publication
0.119
L-tryptophan
-
pH 7.0, 25°C, mutant T342A
0.12
L-tryptophan
-
pH 7.0, 25°C, wild-type enzyme
0.133
L-tryptophan
H55A mutant enzyme, O2 not present at a saturating level
0.18
L-tryptophan
-
pH 7.0, normal atmospheric conditions
0.19
L-tryptophan
-
pH 7.0
0.197
L-tryptophan
H55S mutant enzyme, O2 not present at a saturating level
0.25
L-tryptophan
-
pH 5.5
0.488
L-tryptophan
-
H76A mutant enzyme, pH 8.0, normal atmospheric conditions
0.53
L-tryptophan
-
recombinant isozyme IDO2, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C
0.53
L-tryptophan
-
IDO1, pH and temperature not specified in the publication, cytochrome b5 assay
0.589
L-tryptophan
pH 8.0, temperature not specified in the publication, wild-type enzyme
0.622
L-tryptophan
pH 8.0, temperature not specified in the publication, mutant enzyme N127T
1.29
L-tryptophan
-
Y42F mutant enzyme, pH 8.0, normal atmospheric conditions
2.85
L-tryptophan
pH 8.0, temperature not specified in the publication, mutant enzyme H127E
3.2
L-tryptophan
pH 7.5, 37°C
6.809
L-tryptophan
pH 7.5, 25°C, recombinant enzyme IDO2
7.4
L-tryptophan
pH 7.5, 37°C
12
L-tryptophan
-
recombinant isozyme IDO2, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C
12
L-tryptophan
-
IDO1, pH and temperature not specified in the publication, MB assay
13.6
L-tryptophan
pH 8.0, temperature not specified in the publication, wild-type enzyme
29.9
L-tryptophan
pH 7.0, 37°C
33.9
L-tryptophan
pH 7.5, 37°C
42.7
L-tryptophan
pH 7.0, 37°C
45.9
L-tryptophan
pH 7.5, 37°C
55.4
L-tryptophan
pH 7.5, 37°C
0.037
O2
-
pH 8.0
2.8
O2
-
indoleamine 2,3-dioxygenase
45.7
O2
H55A mutant enzyme
119
O2
25°C, pH 7.5, wild-type enzyme
2.8
oxygen
-
pH 6.5, 37°C
2.8
oxygen
-
pH 6.5, 37°C
0.1
serotonin
-
24°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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]
-
additional information
additional information
bimolecular CO association rate coefficients, 22°C
-
additional information
additional information
-
bimolecular CO association rate coefficients, 22°C
-
additional information
additional information
steadystate, pre-steady-state and stopped-flow kinetics
-
additional information
additional information
stopped-flow and Michaelis-Menten steady-state kinetic measurements, kinetic model for catalytic dioxygenation of L-Trp by hIDO1, detailed overview. At low O2, the reversibility of the first step is essential for accurate reproduction of experimental O2 kcat/KM ratios
-
additional information
additional information
-
stopped-flow and Michaelis-Menten steady-state kinetic measurements, kinetic model for catalytic dioxygenation of L-Trp by hIDO1, detailed overview. At low O2, the reversibility of the first step is essential for accurate reproduction of experimental O2 kcat/KM ratios
-