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Ligand D-tryptophan

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (10 results)

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Show Natural Substrate (10 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.11

D-tryptophan + O2 = N-formyl-D-kynurenine

742114

-

1.13.11.52

D-tryptophan + O2 = N-formyl-D-kynurenine

663820, 665204, 666461, 710831, 664443, 666239, 666378, 666763, 711247, 712947, 724912, 395466, 666138, 395457, 663564, 663995, 663996, 665448, 742114, 711229, 712694, 724429, 741770, 741926, 742005, 742073, 742442, 742634, 742885, 743296, 743654, 713484, 711218, 723923, 726383

-

1.4.3.3

D-Trp + H2O + O2 = indol-3-pyruvate + NH3 + H2O2

743827

1ddo, 3D-view

1.4.3.3

D-Trp + H2O + O2 = indole-3-pyruvate + NH3 + H2O2

743131

1ddo, 3D-view

1.4.3.3

D-tryptophan + H2O + O2 = indol-3-pyruvic acid + NH3 + H2O2

391830, 391865, 391833, 391852, 391861, 391839, 391847

1ddo, 3D-view

1.4.3.3

D-tryptophan + H2O + O2 = indole-3-pyruvic acid + NH3 + H2O2

697313

1ddo, 3D-view

1.4.3.3

4 entries

2.3.1.112

malonyl-CoA + D-tryptophan = CoA + N2-malonyl-D-tryptophan

486140

-

2.3.1.34

acetyl-CoA + D-tryptophan = CoA + acetyl-D-tryptophan

486795

-

2.3.1.36

acetyl-CoA + D-tryptophan = CoA + N-acetyl-D-tryptophan

486807

-

2.3.1.36

propionyl-CoA + D-tryptophan = CoA + N2-propionyl-D-tryptophan

486807

-

2.3.1.36

2 entries

Substrate in Enzyme-catalyzed Reactions (41 results)

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Show Substrate (41 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.11

D-tryptophan + O2 = N-formyl-D-kynurenine

742114

-

1.13.11.26

D-tryptophan + O2 = formylkynurenine

439517, 439522, 439524

-

1.13.11.52

D-Trp + O2 = D-formylkynurenine

671714, 657865

-

1.13.11.52

D-Trp + O2 = N-formyl-D-kynurenine

395463, 395472, 395489, 395459, 395462, 395491, 395480, 395454

-

1.13.11.52

D-tryptophan + O2 = ?

696151

-

1.13.11.52

D-tryptophan + O2 = N-formyl-D-kynurenine

663820, 663910, 665204, 666461, 684391, 710831, 395463, 395472, 659233, 664443, 666239, 666378, 666763, 685239, 698485, 711247, 712947, 724912, 395466, 666138, 395457, 395458, 663564, 663995, 663996, 665448, 665454, 688917, 688457, 742114, 711229, 712694, 724429, 741581, 741770, 741926, 742005, 742073, 742442, 742634, 742885, 743296, 743654, 724301, 665459, 687283, 713484, 711218, 723923, 726383

-

1.13.11.52

4 entries

1.13.99.3

D-tryptophan + O2 = ?

439304, 439307

-

1.14.19.59

D-tryptophan + FADH2 + chloride + O2 + H+ = 6-chloro-D-tryptophan + FAD + 2 H2O

744198

-

1.14.19.59

D-tryptophan + FADH2 + Cl- + O2 + H+ = 6-chloro-D-tryptophan + FAD + 2 H2O

727223

-

1.14.19.59

2 entries

1.14.19.9

D-tryptophan + FADH2 + bromide + O2 + H+ = 7-bromo-D-tryptophan + FAD + 2 H2O

744027

-

1.4.3.3

D-Trp + H2O + O2 = indol-3-pyruvate + NH3 + H2O2

743827, 724401, 655441, 654786, 741688

1ddo, 3D-view

1.4.3.3

D-Trp + H2O + O2 = indole-3-pyruvate + NH3 + H2O2

743131

1ddo, 3D-view

1.4.3.3

D-tryptophan + H2O + O2 = indol-3-pyruvate + NH3 + H2O2

724965, 687891, 763620, 685750

1ddo, 3D-view

1.4.3.3

D-tryptophan + H2O + O2 = indol-3-pyruvic acid + NH3 + H2O2

723920, 391830, 391865, 391833, 391852, 391861, 391839, 391847, 686020, 655558

1ddo, 3D-view

1.4.3.3

D-tryptophan + H2O + O2 = indole-3-pyruvic acid + NH3 + H2O2

697313

1ddo, 3D-view

1.4.99.6

D-tryptophan + H2O + 2,6-dichlorophenolindophenol = 3-indole-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol

394974

-

1.4.99.6

D-tryptophan + H2O + methylene blue = 3-indole-2-oxopropanoate + NH3 + reduced methylene blue

394974

-

1.4.99.6

D-tryptophan + phenazine methosulfate + H2O = 3-indole-2-oxopropanoate + NH3 + reduced phenazine methosulfate

762668

-

1.4.3.3

5 entries

1.4.99.6

3 entries

1.5.99.13

D-tryptophan + oxidized 2,6-dichloroindophenol + H2O = 3-indole-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol

394966

-

2.1.1.106

S-adenosyl-L-methionine + D-tryptophan = S-adenosyl-L-homocysteine + D-2-methyltryptophan

757761

-

2.3.1.112

malonyl-CoA + D-tryptophan = CoA + N2-malonyl-D-tryptophan

486140

-

2.3.1.34

acetyl-CoA + D-tryptophan = CoA + acetyl-D-tryptophan

486795

-

2.3.1.36

acetyl-CoA + D-tryptophan = CoA + N-acetyl-D-tryptophan

657695, 660039, 486807

-

2.3.1.36

propionyl-CoA + D-tryptophan = CoA + N2-propionyl-D-tryptophan

486807

-

2.5.1.34

dimethylallyl diphosphate + D-tryptophan = ?

684649, 701952

-

2.5.1.34

dimethylallyl diphosphate + D-tryptophan = diphosphate + 4-(3-methylbut-2-enyl)-D-tryptophan

673088, 659893, 737544, 737837

-

2.5.1.34

dimethylallyl diphosphate + D-tryptophan = diphosphate + D-4-(3-methylbut-2-enyl)-tryptophan

684649

-

2.5.1.80

dimethylallyl diphosphate + D-tryptophan = ?

701952

-

2.5.1.80

dimethylallyl diphosphate + D-tryptophan = diphosphate + 4-(3-methylbut-2-enyl)-D-tryptophan

737544

-

2.5.1.80

dimethylallyl diphosphate + D-tryptophan = diphosphate + D-7-(3-methylbut-2-enyl)-tryptophan

684649, 688865

-

2.3.1.36

2 entries

2.5.1.34

3 entries

2.5.1.80

3 entries

2.5.1.B44

dimethylallyl diphosphate + D-tryptophan = diphosphate + 1-(2-methylbut-3-en-2-yl)-D-tryptophan

762542

-

2.6.1.21

D-tryptophan + 2-oxoglutarate = 3-indole-2-oxopropanoate + D-glutamate

636738, 636742

-

2.6.1.21

D-tryptophan + pyruvate = 3-indole-2-oxopropanoate + D-alanine

636738, 636742, 759259

-

2.6.1.27

D-tryptophan + 2-oxoglutarate = L-glutamate + 3-indole-2-oxopropanoate

639945

-

2.6.1.27

D-tryptophan + pyruvate = 3-indole-2-oxopropanoate + L-alanine

639941

-

2.6.1.21

2 entries

2.6.1.27

2 entries

2.6.1.74

D-tryptophan + 2-oxoadipate = 3-indole-2-oxopropanoate + 2-aminoadipate

640195

-

4.1.99.1

D-Trp + H2O = indole + pyruvate + NH4+

671054

-

4.3.3.2

D-tryptophan + H2O = ?

679175

-

5.1.1.10

D-Trp = L-Trp

745414

-

5.1.1.10

D-tryptophan = L-tryptophan

744003, 745414

-

5.1.1.10

2 entries

6.3.2.4

ATP + D-Trp = ADP + phosphate + D-Trp-D-Trp

672685

-

Product in Enzyme-catalyzed Reactions (9 results)

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Show Product (9 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.1.43

D-tryptophan methyl ester + H2O = D-tryptophan + methanol

651785

-

3.1.1.96

D-tryptophanyl-tRNATrp + H2O = D-tryptophan + tRNATrp

0

-

3.4.16.4

D-Ala-D-Trp + H2O = D-Ala + D-Trp

0

-

3.5.1.77

N-carbamoyl-D-Trp + H2O = D-Trp + NH3 + CO2

0

-

3.5.1.77

N-carbamoyl-D-tryptophan + H2O = D-tryptophan + NH3 + CO2

0

-

3.5.1.81

N-Acetyl-D-Trp + H2O = acetate + D-Trp

0

-

3.5.1.81

N-acetyl-D-tryptophan + H2O = acetate + D-tryptophan

0

-

5.1.1.10

L-Trp = D-Trp

0

-

5.1.1.10

L-tryptophan = D-tryptophan

0

-

3.5.1.77

2 entries

3.5.1.81

2 entries

5.1.1.10

2 entries

Activator in Enzyme-catalyzed Reactions (6 results)

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Show Activating Compound (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.52

2g subcutaneously

666138

-

1.4.1.15

5 mM, 2.01fold activation

391499

-

4.2.1.1

-

696635, 696648, 702675

-

4.2.1.1

activation constant of 0.0121 mM

702616

-

4.2.1.1

activation constant of 0.019 mM

702683

-

4.2.1.1

high activator

729371

-

4.2.1.1

4 entries

Inhibitor in Enzyme-catalyzed Reactions (18 results)

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Show Inhibitors (18 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.52

-

395454

-

1.13.11.52

no inhibition

395455

-

1.13.11.52

-

663995

-

1.13.11.52

low inhibition

741581

-

1.13.12.3

competitive inhibitor

439347

-

1.13.12.3

weak

439341

-

1.3.3.10

-

639383

-

1.3.3.10

competitive inhibition, Ki: 0.0066 mM

639382

-

1.4.1.20

5 mM, 65% inhibition

349634

-

1.4.1.20

5 mM, 83% inhibition

349634

-

1.13.11.52

4 entries

1.13.12.3

2 entries

1.3.3.10

2 entries

1.4.1.20

2 entries

2.5.1.34

competitive with L-tryptophan

687716

-

3.4.17.1

Ki: 0.014 mM

36360

-

3.5.3.1

-

684384

-

4.1.1.105

non-competitive inhibitor

746086

-

4.1.1.28

-

4221

-

4.1.1.28

non-competitive inhibitor

653443

-

4.1.1.28

2 entries

4.2.1.51

-

33876

-

6.1.1.2

-

299

-

3D Structure of Enzyme-Ligand-Complex (PDB) (10 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (10 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.4.3.3

1ddo, 3D-view

2.3.2.27

6aaw, 3D-view

2.3.2.27

7kjm, 3D-view

2.3.2.27

6aaw, 3D-view

2.3.2.27

7kjm, 3D-view

2.5.1.54

5e5g, 3D-view

2.5.1.54

5e7z, 3D-view

2.5.1.54

5e5g, 3D-view

2.5.1.54

5e7z, 3D-view

2.3.2.27

4 entries

2.5.1.54

4 entries

3.2.1.8

7xna, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (17 results)

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Show Turnover Number (17 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.13.11.52

0.0068

-

-

688917

1.13.11.52

0.0103

-

pH 7.5, 25°C, recombinant enzyme IDO2

741581

1.13.11.52

0.082

-

pH 7.0, 25°C, mutant T342A

724301

1.13.11.52

0.2

-

pH 7.0

687283

1.13.11.52

0.2

-

pH 7.0, 25°C, wild-type enzyme

724301

1.13.11.52

1.18

-

24°C

395462

1.13.11.52

2.07

-

-

395463

1.13.11.52

2.7

-

pH 6.5, 25°C, recombinant enzyme IDO1

741581

1.13.11.52

3.93

-

-

685239

1.13.11.52

5.9

-

-

698485

1.4.3.3

3.2

-

at pH 7.0 and 25°C

723920

1.4.3.3

3.7

-

in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C

724965

1.4.3.3

7.7

-

mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

31

-

mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

33

-

mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

42.4

-

wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.13.11.52

10 entries

1.4.3.3

6 entries

2.5.1.B44

0.0038

-

pH 7.5, 35°C, wild-type enzyme

762542

K_M Value (56 results)

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Show KM Value (56 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.52

0.0019

-

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

659233

1.13.11.52

0.0024

-

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

659233

1.13.11.52

0.0044

-

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

659233

1.13.11.52

0.005

-

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

659233

1.13.11.52

0.0053

-

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

659233

1.13.11.52

0.062

-

pH 7.5, 37 °C, 40 min incubation time

663820

1.13.11.52

0.159

-

pH 7.0, 25°C, mutant T342A

724301

1.13.11.52

0.18

-

pH 7.0

687283

1.13.11.52

0.26

-

pH 7.0, 25°C, wild-type enzyme

724301

1.13.11.52

0.296

-

pH 6.5, 25°C, recombinant enzyme IDO1

741581

1.13.11.52

0.3

-

-

395491

1.13.11.52

0.4

-

-

395489

1.13.11.52

0.4

-

24°C

395462

1.13.11.52

0.44

-

-

688917

1.13.11.52

0.66

-

pH 7.0, 1 mM indole

663996

1.13.11.52

0.83

-

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

663995

1.13.11.52

0.96

-

-

663910

1.13.11.52

1.3

-

pH 7.0, 1 mM 3-indoleethanol

663996

1.13.11.52

1.57

-

-

685239

1.13.11.52

1.7

-

pH 7.0

663996

1.13.11.52

2.6

-

-

698485

1.13.11.52

2.6

-

pH and temperature not specified in the publication

713484

1.13.11.52

2.87

-

-

688457

1.13.11.52

3.609

-

pH 7.5, 25°C, recombinant enzyme IDO2

741581

1.13.11.52

3.795

-

50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37°C, 10 min

666239

1.13.11.52

4.676

-

-

688457

1.13.11.52

5

-

recombinant enzyme

395463

1.13.11.52

5

-

-

395463

1.13.11.52

5.2

-

-

657865

1.13.11.52

5.2

-

37°C, pH 6.5

684391

1.13.11.52

7.3

-

37°C, pH 6.5

684391

1.13.11.52

16

-

pH and temperature not specified in the publication

713484

1.13.11.52

32 entries

1.14.19.59

0.31

-

pH 7.2, 30°C

744198

1.4.3.3

0.17

-

-

391847

1.4.3.3

0.2

-

pH 8.5, 25°C, mutant enzyme Y238S

655441

1.4.3.3

0.3

-

pH 8.5, 25°C, mutant enzyme Y238F

655441

1.4.3.3

0.3

-

pH 8.5, 25°C, wild-type enzyme

655441

1.4.3.3

0.3

-

-

391833

1.4.3.3

0.4

-

pH 7.5, 25°C, mutant enzyme DELTASer308-Lys321

655558

1.4.3.3

0.45

-

mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

0.46

-

mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

0.49

-

wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

0.7

-

immobilized enzyme

391842

1.4.3.3

1.2

-

-

391847

1.4.3.3

1.2

-

free enzyme

391842

1.4.3.3

1.4

-

-

391865

1.4.3.3

1.5

-

at pH 7.0 and 25°C

723920

1.4.3.3

2.7

-

mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

15

-

in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C

724965

1.4.3.3

16 entries

1.4.99.6

0.47

-

both methylene blue and 2,6-dichlorophenolindophenol specific enzymes

394974

2.3.1.112

0.025

-

-

486140

2.3.1.36

4.5

-

-

660039

2.3.1.36

5.5

-

-

486807

2.3.1.36

2 entries

2.5.1.B44

7.94

-

pH 7.5, 35°C, wild-type enzyme

762542

5.1.1.10

1.68

-

pH 7.0, 80°C

745414

5.1.1.10

1.68

-

pH 7.0, 80°C, recombinant enzyme

745414

5.1.1.10

2 entries

K_i Value (6 results)

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Show KI Value (6 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.52

0.05

-

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

663995

1.13.11.52

0.543

-

pH 6.5, 25°C, recombinant enzyme IDO1

741581

1.13.11.52

12

-

pH 6.5, 25°C, recombinant enzyme IDO2

741581

1.13.11.52

3 entries

1.3.3.10

0.0066

-

-

639382, 639383

2.5.1.34

0.0404

-

pH 7.4, 30°C

687716

3.4.17.1

0.014

-

-

36360

IC₅₀ Value (2 results)

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Show IC50 Value (2 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

3.5.3.1

8.4

-

in the presence of 0.5 mM MnCl2, at 37°C

684384

3.5.3.1

10

-

in the presence of 0.5 mM MnCl2, at 37°C

684384

3.5.3.1

2 entries

References & Links

Literature References (139)

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Show Reference (139 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

299

-

Tryptophanyl-tRNA synthetase from beef pancreas

1979

Kisselev, L.L.; Favorova, O.O.; Kovaleva, G.K.

Methods Enzymol.

54

234-257

4221

-

Substrates and Inhibitors of aromatic amino acid decarboxylase

1986

Jung, M.J.

Bioorg. Chem.

14

429-443

33876

-

Regulation of chorismate mutase, prephenate dehydrogenase and prephenate dehydratase of Candida maltosa

1985

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Indoleamine 2,3-dioxygenase 2 (IDO2) and the kynurenine pathway: characteristics and potential roles in health and disease

2013

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Amino Acids

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Molecular basis for the substrate stereoselectivity in tryptophan dioxygenase

2011

Capece, L.; Lewis-Ballester, A.; Marti, M.A.; Estrin, D.A.; Yeh, S.R.

Biochemistry

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Engineering of substrate specificity of D-amino acid oxidase from the yeast Trigonopsis variabilis: directed mutagenesis of Phe258 residue

2012

Komarova, N.V.; Golubev, I.V.; Khoronenkova, S.V.; Chubar, T.A.; Tishkov, V.I.

Biochemistry

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Purification and kinetic characterization of human indoleamine 2,3-dioxygenases 1 and 2 (IDO1 and IDO2) and discovery of selective IDO1 inhibitors

2011

Meininger, D.; Zalameda, L.; Liu, Y.; Stepan, L.P.; Borges, L.; McCarter, J.D.; Sutherland, C.L.

Biochim. Biophys. Acta

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Structure-activity relationship and enzyme kinetic studies on 4-aryl-1H-1,2,3-triazoles as indoleamine 2,3-dioxygenase (IDO) inhibitors

2011

Huang, Q.; Zheng, M.; Yang, S.; Kuang, C.; Yu, C.; Yang, Q.

Eur. J. Med. Chem.

46

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724965

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Is rat an appropriate animal model to study the involvement of D-serine catabolism in schizophrenia? Insights from characterization of D-amino acid oxidase

2011

Frattini, L.F.; Piubelli, L.; Sacchi, S.; Molla, G.; Pollegioni, L.

FEBS J.

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Indole peroxygenase activity of indoleamine 2,3-dioxygenase

2012

Kuo, H.H.; Mauk, A.G.

Proc. Natl. Acad. Sci. USA

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Characterization of a tryptophan 6-halogenase from Streptomyces toxytricini

2011

Zeng, J.; Zhan, J.

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The extremo-alpha-carbonic anhydrase (CA) from Sulfurihydrogenibium azorense, the fastest CA known, is highly activated by amino acids and amines

2013

Akdemir, A.; Vullo, D.; De Luca, V.; Scozzafava, A.; Carginale, V.; Rossi, M.; Supuran, C.T.; Capasso, C.

Bioorg. Med. Chem. Lett.

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737544

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Impacts and perspectives of prenyltransferases of the DMATS superfamily for use in biotechnology

2015

Fan, A.; Winkelblech, J.; Li, S.M.

Appl. Microbiol. Biotechnol.

99

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737837

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A 7-dimethylallyl tryptophan synthase from a fungal Neosartorya sp.: biochemical characterization and structural insight into the regioselective prenylation

2014

Miyamoto, K.; Ishikawa, F.; Nakamura, S.; Hayashi, Y.; Nakanishi, I.; Kakeya, H.

Bioorg. Med. Chem.

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741581

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Human indoleamine 2,3-dioxygenase-2 has substrate specificity and inhibition characteristics distinct from those of indoleamine 2,3-dioxygenase-1

2014

Pantouris, G.; Serys, M.; Yuasa, H.J.; Ball, H.J.; Mowat, C.G.

Amino Acids

46

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741688

25217016

A highly stable d-amino acid oxidase of the thermophilic bacterium Rubrobacter xylanophilus

2014

Takahashi, S.; Furukawara, M.; Omae, K.; Tadokoro, N.; Saito, Y.; Abe, K.; Kera, Y.

Appl. Environ. Microbiol.

80

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741770

25712221

Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen

2015

Kolawole, A.O.; Hixon, B.P.; Dameron, L.S.; Chrisman, I.M.; Smirnov, V.V.

Arch. Biochem. Biophys.

570

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741926

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Structural study of a flexible active site loop in human indoleamine 2,3-dioxygenase and its functional implications

2016

Alvarez, L.; Lewis-Ballester, A.; Roitberg, A.; Estrin, D.A.; Yeh, S.R.; Marti, M.A.; Capece, L.

Biochemistry

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742005

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Substrate binding in human indoleamine 2,3-dioxygenase 1 a spectroscopic analysis

2017

Nienhaus, K.; Nickel, E.; Nienhaus, G.U.

Biochim. Biophys. Acta

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742073

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Discovery and structure-activity relationships of phenyl benzenesulfonylhydrazides as novel indoleamine 2,3-dioxygenase inhibitors

2014

Cheng, M.F.; Hung, M.S.; Song, J.S.; Lin, S.Y.; Liao, F.Y.; Wu, M.H.; Hsiao, W.; Hsieh, C.L.; Wu, J.S.; Chao, Y.S.; Shih, C.; Wu, S.Y.; Ueng, S.H.

Bioorg. Med. Chem. Lett.

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742114

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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

2014

Maeta, A.; Sano, M.; Fukuwatari, T.; Funakoshi, H.; Nakamura, T.; Shibata, K.

Biosci. Biotechnol. Biochem.

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Discovery and evaluation of inhibitors to the immunosuppressive enzyme indoleamine 2,3-dioxygenase 1 (IDO1) probing the active site-inhibitor interactions

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Tomek, P.; Palmer, B.D.; Flanagan, J.U.; Sun, C.; Raven, E.L.; Ching, L.M.

Eur. J. Med. Chem.

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Indoleamine 2,3-dioxygenase depletes tryptophan, activates general control non-derepressible 2 kinase and down-regulates key enzymes involved in fatty acid synthesis in primary human CD4+ T cells

2015

Eleftheriadis, T.; Pissas, G.; Antoniadi, G.; Liakopoulos, V.; Stefanidis, I.

Immunology

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Substrate oxidation by indoleamine 2,3-dioxygenase evidence for a common reaction mechanism

2015

Booth, E.S.; Basran, J.; Lee, M.; Handa, S.; Raven, E.L.

J. Biol. Chem.

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Role of D-amino acid oxidase in the production of kynurenine pathway metabolites from D-tryptophan in mice

2015

Notarangelo, F.M.; Wang, X.D.; Horning, K.J.; Schwarcz, R.

J. Neurochem.

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Indoleamine 2,3-dioxygenase regulates T cell activity through Vav1/Rac pathway

2017

Li, R.; Li, H.; Sun, Q.; Liu, L.; Zhang, C.; Ren, X.

Mol. Immunol.

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743654

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Effects of various phytochemicals on indoleamine 2,3-dioxygenase 1 activity galanal is a novel, competitive inhibitor of the enzyme

2014

Yamamoto, R.; Yamamoto, Y.; Imai, S.; Fukutomi, R.; Ozawa, Y.; Abe, M.; Matuo, Y.; Saito, K.

PLoS ONE

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743827

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pH-Dependent enantioselectivity of D-amino acid oxidase in aqueous solution

2017

Liu, Q.; Chen, L.; Zhang, Z.; Du, B.; Xiao, Y.; Yang, K.; Gong, L.; Wu, L.; Li, X.; He, Y.

Sci. Rep.

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Identification of a novel amino acid racemase from a hyperthermophilic archaeon Pyrococcus horikoshii OT-3 induced by D-amino acids

2015

Kawakami, R.; Ohmori, T.; Sakuraba, H.; Ohshima, T.

Amino Acids

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Enzymatic halogenation of tryptophan on a gram scale

2015

Frese, M.; Sewald, N.

Angew. Chem. Int. Ed. Engl.

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A flavin-dependent tryptophan 6-halogenase and its use in modification of pyrrolnitrin biosynthesis

2006

Seibold, C.; Schnerr, H.; Rumpf, J.; Kunzendorf, A.; Hatscher, C.; Wage, T.; Ernyei, A.; Dong, C.; Naismith, J.; van Pee, K.

Biocatal. Biotransform.

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First characterization of an archaeal amino acid racemase with broad substrate specificity from the hyperthermophile Pyrococcus horikoshii OT-3

2017

Kawakami, R.; Sakuraba, H.; Ohmori, T.; Ohshima, T.

J. Biosci. Bioeng.

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Tryptophan decarboxylase from Catharanthus roseus cell suspension cultures purification, molecular and kinetic data of the homogenous protein

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Noe, W.; Mollenschott, C.; Berlin, J.

Plant Mol. Biol.

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The thiostrepton A tryptophan methyltransferase TsrM catalyses a cob(II)alamin-dependent methyl transfer reaction

2015

Benjdia, A.; Pierre, S.; Gherasim, C.; Guillot, A.; Carmona, M.; Amara, P.; Banerjee, R.; Berteau, O.

Nat. Commun.

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AtDAT1 is a key enzyme of D-amino acid stimulated ethylene production in Arabidopsis thaliana

2019

Suarez, J.; Hener, C.; Lehnhardt, V.A.; Hummel, S.; Stahl, M.; Kolukisaoglu, U.e.

Front. Plant Sci.

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Biochemical and mechanistic characterization of the fungal reverse N-1-dimethylallyltryptophan synthase DMATS1Ff

2019

Burkhardt, I.; Ye, Z.; Janevska, S.; Tudzynski, B.; Dickschat, J.S.

ACS Chem. Biol.

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Amine oxidation by D-arginine dehydrogenase in Pseudomonas aeruginosa

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Ouedraogo, D.; Ball, J.; Iyer, A.; Reis, R.A.G.; Vodovoz, M.; Gadda, G.

Arch. Biochem. Biophys.

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Modulating D-amino acid oxidase (DAAO) substrate specificity through facilitated solvent access

2018

Subramanian, K.; Gora, A.; Spruijt, R.; Mitusinska, K.; Suarez-Diez, M.; Martins Dos Santos, V.; Schaap, P.J.

PLoS ONE

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