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Ligand 5-hydroxy-L-tryptophan

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 5-hydroxy-L-tryptophan

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Natural Substrate (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.52

5-hydroxy-L-tryptophan + O2 = N-formyl-5-hydroxy-L-kynurenine

712947, 663564

-

4.1.1.105

5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2

744703

-

4.1.1.28

5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2

745120, 746908, 747840

-

4.1.1.28

5-hydroxy-L-tryptophan = serotonin + CO2

692593, 690973

-

4.1.1.28

5-hydroxytryptophan = 5-hydroxytryptamine + CO2

693382, 691987

-

4.1.1.28

5-Hydroxytryptophan = Serotonin + CO2

692189, 693490, 704803, 705756, 694106, 691846, 693374

-

4.1.1.28

L-5-hydroxytryptophan = serotonin + CO2

694362

-

4.1.1.28

5 entries

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

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Show Natural Product (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.16.4

L-tryptophan + (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin

0

-

1.14.16.4

L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin

0

-

1.14.16.4

L-tryptophan + tetrahydropteridine + O2 = 5-hydroxy-L-tryptophan + dihydropteridine + H2O

0, 438666, 438654, 438656, 438667, 438658

-

1.14.16.4

3 entries

Substrate in Enzyme-catalyzed Reactions (37 results)

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Show Substrate (37 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.26

L-5-hydroxytryptophan + O2 = 5-hydroxy-N-formylkynurenine

439517

-

1.13.11.52

5-hydroxy-L-tryptophan + O2 = (2S)-4-(2-amino-5-hydroxyphenyl)-2-(formylamino)-4-oxobutanoic acid

684391

-

1.13.11.52

5-hydroxy-L-tryptophan + O2 = 5-hydroxy-N-formyl-L-kynurenine

741581, 742885

-

1.13.11.52

5-hydroxy-L-tryptophan + O2 = ?

395472, 666239

-

1.13.11.52

5-hydroxy-L-tryptophan + O2 = N-formyl-5-hydroxy-L-kynurenine

710831, 395463, 659233, 712173, 712947, 663564

-

1.13.11.52

5-hydroxy-tryptophan + O2 = 4-(2-amino-5-hydroxyphenyl)-2-(formylamino)-4-oxobutanoic acid

685239

-

1.13.11.52

5-hydroxytryptophan + O2 = ?

696151

-

1.13.11.52

5-hydroxytryptophan + O2- = N-formyl-5-hydroxykynurenine

665454

-

1.13.11.52

L-5-hydroxytryptophan + O2 = ?

395463, 395472, 395459, 395462

-

1.13.11.52

8 entries

1.13.12.3

5-hydroxytryptophan + O2 = 5-hydroxyindole-3-acetamide + CO2 + H2O

439341

-

1.13.99.3

5-hydroxy-L-tryptophan + O2 = ?

439309

-

1.14.19.9

5-hydroxy-L-tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-5-hydroxy-L-tryptophan + FAD + 2 H2O

744712, 744027

-

1.16.3.1

5-hydroxytryptophan + Fe2+ + O2 = ?

438006

-

2.1.1.106

S-adenosyl-L-methionine + L-5-hydroxy-tryptophan = S-adenosyl-L-homocysteine + L-5-hydroxy-2-methyltryptophan

757761

-

2.5.1.34

dimethylallyl diphosphate + 5-hydroxy-L-tryptophan = diphosphate + 4-(3-methylbut-2-enyl)-5-hydroxy-L-tryptophan

673088

-

2.5.1.34

dimethylallyl diphosphate + 5-hydroxy-L-tryptophan = diphosphate + 5-hydroxy-4-(3-methylbut-2-enyl)-L-tryptophan

687716, 684649, 737544, 737837

-

2.5.1.80

dimethylallyl diphosphate + 5-hydroxy-L-tryptophan = diphosphate + 5-hydroxy-4-(3-methylbut-2-enyl)-L-tryptophan

737544

-

2.5.1.80

dimethylallyl diphosphate + 5-hydroxy-L-tryptophan = diphosphate + 5-hydroxy-7-(3-methylbut-2-enyl)-L-tryptophan

684649

-

2.5.1.34

2 entries

2.5.1.80

2 entries

2.5.1.B44

dimethylallyl diphosphate + 5-hydroxy-L-tryptophan = diphosphate + 5-hydroxy-1-(2-methylbut-3-en-2-yl)-L-tryptophan

762542

-

2.6.1.27

5-hydroxytryptophan + 2-oxoglutarate = 3-(5-hydroxyindole)-2-oxopropanoate + L-glutamate

639946, 639938

-

2.6.1.27

5-hydroxytryptophan + oxaloacetate = 3-(5-hydroxyindole)-2-oxopropanoate + L-aspartate

639946

-

2.6.1.27

2 entries

2.6.1.51

5-hydroxytryptophan + pyruvate = 3-(5-hydroxyindole)-2-oxopropanoate + alanine

640136, 640135

-

2.6.1.57

5-hydroxytryptophan + 2-oxoglutarate = 3-(5-hydroxyindole)-2-oxopropanoate + L-glutamate

636646

-

2.6.1.60

5-hydroxytryptophan + glyoxylate = 3-(5-hydroxyindole)-2-oxopropanoate + glycine

636995

-

2.6.1.63

5-hydroxytryptophan + glyoxylate = 3-(5-hydroxyindole)-2-oxopropanoate + glycine

636995, 636996

-

4.1.1.105

5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2

746086, 744703, 749265

-

4.1.1.28

5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2

744252, 745120, 653443, 746908, 747840

-

4.1.1.28

5-hydroxy-L-tryptophan = ?

743976

-

4.1.1.28

5-hydroxy-L-tryptophan = serotonin + CO2

680070, 677950, 680090, 681181, 681948, 650410, 677584, 692593, 690973

-

4.1.1.28

5-hydroxytryptophan = 5-hydroxytryptamine + CO2

693382, 650868, 653346, 653443, 691987

-

4.1.1.28

5-Hydroxytryptophan = Serotonin + CO2

4210, 4213, 4226, 692189, 693490, 704803, 705756, 4200, 4204, 4231, 703136, 4218, 4215, 4203, 694106, 691846, 4216, 693374

-

4.1.1.28

L-5-hydroxytryptophan = 5-hydroxytryptamine + CO2

649696

-

4.1.1.28

L-5-hydroxytryptophan = serotonin + CO2

694362, 705265

-

4.1.1.28

7 entries

4.1.1.53

5-Hydroxytryptophan = Serotonin + CO2

4231, 4708, 4704

-

4.1.99.1

5-hydroxy-L-Trp + H2O = ?

37356, 37363, 37349

-

6.1.1.2

ATP + 5-hydroxy-L-tryptophan + tRNATrp = AMP + diphosphate + 5-hydroxy-L-tryptophan-tRNATrp

663230

1yia, 3D-view

6.1.1.2

ATP + 5-hydroxytryptophan + tRNATrp = AMP + diphosphate + 5-hydroxytryptophyl-tRNATrp

691148

-

6.1.1.2

2 entries

Product in Enzyme-catalyzed Reactions (14 results)

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Show Product (14 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.16.1

L-tryptophan + 5,6,7,8-tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin

0

-

1.14.16.1

L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxytryptophan + 4a-hydroxytetrahydrobiopterin

0

-

1.14.16.4

L-tryptophan + (6R)-L-erytho-5,6,7,8-tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + ?

0

-

1.14.16.4

L-tryptophan + (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin

0

-

1.14.16.4

L-tryptophan + 6-methyl-tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 6-methyl-4a-hydroxytetrahydrobiopterin

0

-

1.14.16.4

L-tryptophan + 6-methyl-tetrahydropterin + O2 = 5-hydroxy-L-tryptophan + 6-methyl-4a-hydroxytetrahydropterin

0

-

1.14.16.4

L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin

0

-

1.14.16.4

L-tryptophan + tetrahydrobiopterin = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin

0

-

1.14.16.4

L-tryptophan + tetrahydropteridine + O2 = 5-hydroxy-L-tryptophan + dihydropteridine + H2O

438666, 438657, 438661, 438664, 438654, 438655, 438659, 438662, 438663, 438667, 438660, 438672, 438673, 438671, 438665, 438668, 438658, 438656, 0

-

4.1.99.1

5-hydroxyindole + L-Cys = 5-hydroxy-L-Trp + ?

0

-

4.1.99.1

5-hydroxyindole + S-methyl-L-Cys = 5-hydroxy-L-Trp + ?

0

-

1.14.16.1

2 entries

1.14.16.4

7 entries

4.1.99.1

2 entries

4.2.1.122

L-serine + 5-hydroxyindole = 5-hydroxy-L-tryptophan + H2O

0

-

4.2.1.20

L-serine + 5-hydroxyindole = 5-hydroxy-L-tryptophan + H2O

0

-

4.2.1.20

L-serine + 5-hydroxyindole = 5-hydroxytryptophan + H2O

0

-

4.2.1.20

2 entries

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.87

activates, best at 0.1 mM

719583

-

Inhibitor in Enzyme-catalyzed Reactions (20 results)

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Show Inhibitors (20 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.52

-

657865

-

1.13.11.52

0.1 mM, 40% inhibition of cleavage of D-tryptophan, 53% inhibition of cleavage of L-tryptophan

663910

-

1.13.11.52

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, 37°C, 10 min

666239

-

1.13.11.52

1 mM, 78.6% inhibition

687095

-

1.13.11.52

-

395452

-

1.13.11.52

5 entries

1.13.12.16

-

639224

-

1.14.16.4

-

438661

-

1.14.16.4

0.018 mM, 50% inhibition

438673

-

1.14.16.4

-

438675

-

1.14.16.4

3 entries

1.14.18.1

-

636364

-

1.2.1.3

23% inhibition at 0.1 mM

692623

-

1.3.3.10

-

639383

-

1.3.3.10

competitive inhibition, Ki: 0.037 mM

639382

-

1.3.3.10

2 entries

2.6.1.5

30% inhibition with tyrosine at 3 mM and 5-hydroxytryptophan at 12 mM

640109

-

3.5.3.1

-

684384

-

4.1.1.28

strong inhibitory effect of 5-hydroxy-L-tryptophan on the conversion of 3,4-dihydroxyphenylalanine

681948

-

4.1.1.28

substrate inhibition

690973

-

4.1.1.28

-

4203, 4228

-

4.1.1.28

3 entries

4.1.1.53

complete inhibition at 0.001 mM

4704

-

6.1.1.2

ATP-diphosphate exchange, weak

299

-

3D Structure of Enzyme-Ligand-Complex (PDB) (2 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (2 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.7.10.1

7ofv, 3D-view

6.1.1.2

1yia, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (16 results)

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Show Turnover Number (16 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.13.11.52

0.025

-

pH 6.5, 25°C, recombinant enzyme IDO1

741581

1.13.11.52

0.025

-

-

685239

1.13.11.52

0.0433

-

24°C

395462

1.13.11.52

0.065

-

-

395463

2.5.1.34

0.165

-

in 50 mM Tris/HCl (pH 7.5) with 5 mM CaCl2

673088

2.5.1.34

0.56

-

pH 7.4, 30°C

687716

1.13.11.52

4 entries

2.5.1.34

2 entries

2.5.1.B44

2.26

-

pH 7.5, 35°C, wild-type enzyme

762542

4.1.1.105

0.16

-

mutant enzyme G351S, at pH 7.5 and 37°C

744703

4.1.1.105

0.17

-

recombinant wild-type enzyme, pH 7.5, 37°C

744703

4.1.1.105

0.17

-

wild type enzyme, at pH 7.5 and 37°C

744703

4.1.1.105

0.26

-

mutant enzyme G351L, at pH 7.5 and 37°C

744703

4.1.1.28

0.67

-

wild-type enzyme

690973

4.1.1.28

0.99

-

pH 7.5, 25°C, anaerobiosis

649696

4.1.1.28

1.99

-

pH 7.5, 25°C, aerobiosis

649696

4.1.1.28

2.94

-

pH 7.5, 25°C, aerobiosis

649696

4.1.1.28

6.08

-

pH 7.5, 25°C, anaerobiosis

649696

4.1.1.105

4 entries

4.1.1.28

5 entries

K_M Value (34 results)

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Show KM Value (34 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.52

0.017

-

pH 6.5, 25°C, recombinant enzyme IDO1

741581

1.13.11.52

0.017

-

-

685239

1.13.11.52

0.02

-

24°C

395462

1.13.11.52

0.1

-

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

0.1

-

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

0.14

-

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

0.17

-

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

0.21

-

37°C, pH 6.5

684391

1.13.11.52

0.4

-

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

0.44

-

-

395463

1.13.11.52

0.44

-

recombinant enzyme

395463

1.13.11.52

0.68

-

37°C, pH 6.5

684391

1.13.11.52

12 entries

1.16.3.1

0.0163

-

-

438006

2.5.1.34

0.3031

-

pH 7.4, 30°C

687716

2.5.1.34

0.509

-

in 50 mM Tris/HCl (pH 7.5) with 5 mM CaCl2

673088

2.5.1.34

2 entries

2.5.1.B44

5.61

-

pH 7.5, 35°C, wild-type enzyme

762542

4.1.1.105

0.32

-

recombinant wild-type enzyme, pH 7.5, 37°C

744703

4.1.1.105

0.32

-

wild type enzyme, at pH 7.5 and 37°C

744703

4.1.1.105

0.35

-

mutant enzyme G351S, at pH 7.5 and 37°C

744703

4.1.1.105

1.3

-

at pH 7.5, temperature not specified in the publication

746086

4.1.1.105

1.72

-

mutant enzyme G351L, at pH 7.5 and 37°C

744703

4.1.1.105

1.72

-

recombinant mutant G351L, pH 7.5, 37°C

744703

4.1.1.28

0.016

-

-

4226

4.1.1.28

0.02

-

-

4210

4.1.1.28

0.038

-

pH 7.5, 25°C, anaerobiosis

649696

4.1.1.28

0.047

-

in the presence of 0.07 mM pyridoxal 5'-phosphate, in 167 mM sodium phosphate pH 8.0, at 37°C

705265

4.1.1.28

0.049

-

wild-type enzyme

690973

4.1.1.28

0.053

-

in the absence of pyridoxal 5'-phosphate

705265

4.1.1.28

0.155

-

pH 7.5, 25°C, aerobiosis

649696

4.1.1.28

0.23

-

-

4218

4.1.1.28

0.23

-

pH 7.0, 32°C

653346

4.1.1.28

0.49

-

in 167 mM phosphate buffer, pH 7.0, containing 39 mM dithiotreitol and 0.167 mM NaEDTA, for 2 h at 37°C

681948

4.1.1.105

6 entries

4.1.1.28

10 entries

4.1.1.53

0.002

-

-

4704

4.1.99.1

2.7

-

alpha,beta-elimination

37352

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

0.001

-

-

395452

1.13.11.52

0.01

-

-

395452

1.13.11.52

0.072

-

-

657865

1.13.11.52

3 entries

1.14.16.4

0.035

-

-

438675

1.3.3.10

0.037

-

-

639382, 639383

4.1.1.28

5.7

-

wild-type enzyme, the data of initial velocity for decarboxylation of 5-hydroxy-L-tryptophan versus substrate concentration exhibit a substrate-inhibition pattern that requires a modified version of the Michaelis-Menten equation.

690973

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

3.6

-

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

684384

3.5.3.1

3.9

-

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

684384

3.5.3.1

2 entries

References & Links

Literature References (120)

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Show Reference (120 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

4200

4536745

On the identity of DOPA decarboxylase and 5-hydroxytryptophan decarboxylase

1972

Christenson, J.G.; Dairman, W.; Udenfrien, S.

Proc. Natl. Acad. Sci. USA

69

343-347

4203

-

Partial purification and some properties of tryptophan decarboxylase from Phalaris tuberosa

1972

Baxter, C.; Slaytor, M.

Phytochemistry

11

2763-2766

4204

21822

Aromatic amino acid decarboxylase: pH-dependence of substrates and inhibitors

1977

Bender, D.A.; Coulson, W.F.

Biochem. Soc. Trans.

5

1353-1356

4210

-

Aromatic L-amino acid decarboxylase (guinea pig kidney)

1971

Lovenberg, W.

Methods Enzymol.

17B

652-656

4213

309771

Substrate specificity and other properties of dopa decarboxylase from guinea pig kidneys

1978

Srinivasan, K.; Awapara, J.

Biochim. Biophys. Acta

526

597-604

4215

39668

Biochemical properties and kinetic parameters of dihydroxyphenylalanine-5-hydroxytryptophan decarboxylase in brain, liver, and adrenals of cat

1979

Bouchard, S.; Roberge, A.G.

Can. J. Biochem.

57

1014-1018

4216

-

Aromatic L-amino acid decarboxylase from Micrococcus percitreus. Purification, crystallization and properties

1981

Nakazawa, H.; Kumagai, H.; Yamada, H.

Agric. Biol. Chem.

45

2543-2552

4218

3600369

Aromatic-L-amino acid decarboxylase from pig kidney

1987

Voltattorni, C.B.; Giartosio, A.; Turano, C.

Methods Enzymol.

142

179-187

4226

2117047

Characterization of recombinant human aromatic L-amino acid decarboxylase expressed in COS cells

1990

Sumi, C.; Ichinose, H.; Nagatsu, T.

J. Neurochem.

55

1075-1078

4228

2374548

Purification and characterization of L-DOPA decarboxylase from human kidney

1990

Mappouras, D.G.; Stiakakis, J.; Fragoulis, E.G.

Mol. Cell. Biochem.

94

147-156

4231

9367815

Expression, purification, and characterization of rat aromatic L-amino acid decarboxylase in Escherichia coli

1997

Jebai, F.; Hanoun, N.; Hamon, M.; Thibault, J.; Peltre, G.; Gros, F.; Krieger, M.

Protein Expr. Purif.

11

185-194

4704

14466899

Aromatic L-amino acid decarboxylase

1962

Lovenberg, W.; Weissbach, H.; Udenfriend, S.

J. Biol. Chem.

237

89-93

4708

-

Distribution and formation of aromatic L-amino acid decarboxylase in bacteria

1977

Nakazawa, H.; Sano, K.; Kumagai, H.; Yamada, H.

Agric. Biol. Chem.

41

2241-2247

37349

-

Purification, crystallization and properties of tryptophanase from Proteus rettgeri

1974

Yoshida, H.; Utagawa, T.; Kumagai, H.; Yamada, H.

Agric. Biol. Chem.

38

2065-2072

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Mammalian dopa decarboxylase structure, catalytic activity and inhibition

2014

Bertoldi, M.

Arch. Biochem. Biophys.

546

1-7

747840

29225571

Heterogenic distribution of aromatic L-amino acid decarboxylase neurons in the rat spinal cord

2017

Ren, L.Q.; Chen, M.; Hultborn, H.; Guo, S.; Zhang, Y.; Zhang, M.

Front. Integr. Neurosci.

11

31

749265

26795344

Withania coagulans tryptophan decarboxylase gene cloning, heterologous expression, and catalytic characteristics of the recombinant enzyme

2017

Jadaun, J.S.; Sangwan, N.S.; Narnoliya, L.K.; Tripathi, S.; Sangwan, R.S.

Protoplasma

254

181-192

757761

26456915

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.

6

8377

762542

31756078

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.

14

2922-2931

Links to other databases for 5-hydroxy-L-tryptophan

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