Information on EC 1.4.1.19 - tryptophan dehydrogenase

Substrates: no activity with D-tryptophan
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: amination proceeds more intensively than deamination
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: no activity with D-tryptophan
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: no activity with D-tryptophan
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: amination proceeds more intensively than deamination
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: no activity with D-tryptophan
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: amination proceeds more intensively than deamination
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
Products: -

L-tryptophan + NAD+ + H2O

(indol-3-yl)pyruvate + NH3 + NADH + H+

741706, 742947

Substrates: -
Products: -

L-tryptophan + NAD+ + H2O

(indol-3-yl)pyruvate + NH3 + NADH + H+

Substrates: the enzyme is highly specific for the deamination of amino acid L-tryptophan
Products: -

L-tryptophan + NAD+ + H2O

(indol-3-yl)pyruvate + NH3 + NADH + H+

Substrates: -
Products: -

L-tryptophan + NAD+ + H2O

(indol-3-yl)pyruvate + NH3 + NADH + H+

Substrates: the enzyme is highly specific for the deamination of amino acid L-tryptophan
Products: -

L-tryptophan + NAD+ + H2O

(indol-3-yl)pyruvate + NH3 + NADH + H+

Substrates: -
Products: -

additional information

Substrates: the enzyme shows no activity with D-tryptophan, L-tyrosine, L-alanine, L-valine, L-leucine, L-isoleucine, L-proline, L-cystine, L-methionine, L-asparagine, L-glutamine, L-aspartic acid, L-glutamic acid, L-serine, L-threonine, L-histine, L-arginine, L-lysine, glcyine, phenylpyruvate, NADP+, and NADPH
Products: -

additional information

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

(indol-3-yl)pyruvate + NH3 + NADH + H+

L-tryptophan + NAD+ + H2O

4 entries

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

5 entries

L-tryptophan + NAD+ + H2O

(indol-3-yl)pyruvate + NH3 + NADH + H+

5 entries

(indol-3-yl)pyruvate + NH3 + NADH + H+

L-tryptophan + NAD+ + H2O

Substrates: -
Products: -

(indol-3-yl)pyruvate + NH3 + NADH + H+

L-tryptophan + NAD+ + H2O

Substrates: -
Products: -

(indol-3-yl)pyruvate + NH3 + NADH + H+

L-tryptophan + NAD+ + H2O

Substrates: -
Products: -

(indol-3-yl)pyruvate + NH3 + NADH + H+

L-tryptophan + NAD+ + H2O

Substrates: -
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
Products: -

L-tryptophan + NAD(P)+

indol-3-yl-pyruvate + NH3 + NAD(P)H

Substrates: primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
Products: -

L-tryptophan + NAD+ + H2O

(indol-3-yl)pyruvate + NH3 + NADH + H+

741706, 742947

Substrates: -
Products: -

L-tryptophan + NAD+ + H2O

(indol-3-yl)pyruvate + NH3 + NADH + H+

Substrates: the enzyme is highly specific for the deamination of amino acid L-tryptophan
Products: -

L-tryptophan + NAD+ + H2O

(indol-3-yl)pyruvate + NH3 + NADH + H+

Substrates: -
Products: -

L-tryptophan + NAD+ + H2O

(indol-3-yl)pyruvate + NH3 + NADH + H+

Substrates: the enzyme is highly specific for the deamination of amino acid L-tryptophan
Products: -

L-tryptophan + NAD+ + H2O

(indol-3-yl)pyruvate + NH3 + NADH + H+

Substrates: -
Products: -

show all columns Go to Cofactor Search

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

NAD(P)+

NAD(P)H

NAD+

NADH

NAD(P)+

NAD(P)+

NAD(P)+

NAD(P)+

NAD(P)+

NAD(P)+

NAD(P)H

NAD(P)H

NAD(P)H

NAD(P)H

NAD(P)H

effect of NADPH compared to NADH is distinctly higher

NAD(P)H

show all columns Go to Metals and Ions Search

normal Nicotiana tabacum cells: higher specific activity with NADPH than with NADH, tumor cells of Nicotiana tabacum: no difference in specific activity with NADPH and NADH

NAD+

NAD+

NADH

NADH

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Ca2+

2 entries

Mn2+

activation

additional information

Ca2+

Ca2+

optimal activation at 0.8 mM

additional information

the enzyme is not activated by metal ions

additional information

absence of heavy metal ions in active centre

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

(indol-3-yl)pyruvate

substrate inhibition

EDTA

reactivation by Ca2+ and Mn2+

additional information

presence of a carbonyl group in the active centre, less sensitive to SH-inhibitors than glutamate dehydrogenase

show all columns Go to Activating Compound Search

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

additional information

not influenced by EDTA (10 mM), KCl (100 mM) or DMSO (1% (v/v))

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.014

(indol-3-yl)pyruvate

at pH 7.5 and 25°C

0.017 - 1.1

L-tryptophan

21 entries

0.025

NAD+

at pH 11.0 and 25°C

0.038 - 1.46

NADH

4 entries

130

NH3

at pH 7.5 and 25°C

0.017

L-tryptophan

mutant enzyme V132A, at pH 11.0 and 25°C

0.019

L-tryptophan

mutant enzyme V133A, at pH 11.0 and 25°C

0.021

L-tryptophan

mutant enzyme Y292H, at pH 11.0 and 25°C

0.03

L-tryptophan

mutant enzyme Y292W, at pH 11.0 and 25°C

0.031

L-tryptophan

at pH 11.0 and 25°C

0.039

L-tryptophan

mutant enzyme Y292F, at pH 11.0 and 25°C

0.045

L-tryptophan

wild type enzyme, at pH 11.0 and 25°C

0.047

L-tryptophan

mutant enzyme M295A, at pH 11.0 and 25°C

0.047

L-tryptophan

mutant enzyme M40L, at pH 11.0 and 25°C

0.047

L-tryptophan

mutant enzyme V291A, at pH 11.0 and 25°C

0.059

L-tryptophan

mutant enzyme I296A, at pH 11.0 and 25°C

0.194

L-tryptophan

mutant enzyme L59F, at pH 11.5 and 30°C

0.2

L-tryptophan

mutant enzyme M65A, at pH 11.0 and 25°C

0.201

L-tryptophan

wild type enzyme, at pH 11.5 and 30°C

0.221

L-tryptophan

mutant enzyme D168G, at pH 11.5 and 30°C

0.228

L-tryptophan

mutant enzyme I296N, at pH 11.5 and 30°C

0.268

L-tryptophan

mutant enzyme L59F/D168G/A234D/I296N, at pH 11.5 and 30°C

0.288

L-tryptophan

mutant enzyme A234D, at pH 11.5 and 30°C

0.52

L-tryptophan

mutant enzyme L288M, at pH 11.0 and 25°C

0.82

L-tryptophan

mutant enzyme A69M, at pH 11.0 and 25°C

1.1

L-tryptophan

mutant enzyme A69L, at pH 11.0 and 25°C

0.038

NADH

at pH 7.5 and 25°C

1.36

NADH

tumor C-58 cell culture

1.39

NADH

tumor T-24 cell culture

1.46

NADH

normal cell culture

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

(indol-3-yl)pyruvate

at pH 7.5 and 25°C

0.39 - 21

L-tryptophan

15 entries

4.3

NAD+

at pH 11.0 and 25°C

NADH

at pH 7.5 and 25°C

NH3

at pH 7.5 and 25°C

0.39

L-tryptophan

mutant enzyme L288M, at pH 11.0 and 25°C

1.1

L-tryptophan

mutant enzyme M65A, at pH 11.0 and 25°C

1.2

L-tryptophan

mutant enzyme A69L, at pH 11.0 and 25°C

1.2

L-tryptophan

mutant enzyme A69M, at pH 11.0 and 25°C

2.6

L-tryptophan

mutant enzyme V133A, at pH 11.0 and 25°C

2.9

L-tryptophan

mutant enzyme V291A, at pH 11.0 and 25°C

3.5

L-tryptophan

mutant enzyme Y292H, at pH 11.0 and 25°C

4.2

L-tryptophan

at pH 11.0 and 25°C

4.6

L-tryptophan

mutant enzyme V132A, at pH 11.0 and 25°C

L-tryptophan

mutant enzyme M295A, at pH 11.0 and 25°C

8.5

L-tryptophan

mutant enzyme Y292W, at pH 11.0 and 25°C

L-tryptophan

mutant enzyme I296A, at pH 11.0 and 25°C

L-tryptophan

mutant enzyme M40L, at pH 11.0 and 25°C

L-tryptophan

wild type enzyme, at pH 11.0 and 25°C

L-tryptophan

mutant enzyme Y292F, at pH 11.0 and 25°C

show all columns Go to kcat/KM Value Search

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

1100

(indol-3-yl)pyruvate

at pH 7.5 and 25°C

0.75 - 540

L-tryptophan

15 entries

170

NAD+

at pH 11.0 and 25°C

550

NADH

at pH 7.5 and 25°C

0.13

NH3

at pH 7.5 and 25°C

0.75

L-tryptophan

mutant enzyme L288M, at pH 11.0 and 25°C

1.1

L-tryptophan

mutant enzyme A69L, at pH 11.0 and 25°C

1.5

L-tryptophan

mutant enzyme A69M, at pH 11.0 and 25°C

5.5

L-tryptophan

mutant enzyme M65A, at pH 11.0 and 25°C

L-tryptophan

mutant enzyme V291A, at pH 11.0 and 25°C

140

L-tryptophan

at pH 11.0 and 25°C

140

L-tryptophan

mutant enzyme V133A, at pH 11.0 and 25°C

170

L-tryptophan

mutant enzyme I296A, at pH 11.0 and 25°C

170

L-tryptophan

mutant enzyme M295A, at pH 11.0 and 25°C

170

L-tryptophan

mutant enzyme Y292H, at pH 11.0 and 25°C

260

L-tryptophan

mutant enzyme M40L, at pH 11.0 and 25°C

270

L-tryptophan

mutant enzyme V132A, at pH 11.0 and 25°C

280

L-tryptophan

mutant enzyme Y292W, at pH 11.0 and 25°C

440

L-tryptophan

wild type enzyme, at pH 11.0 and 25°C

540

L-tryptophan

mutant enzyme Y292F, at pH 11.0 and 25°C

show all columns Go to Ki Value Search

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.014

(indol-3-yl)pyruvate

at pH 11.0 and 25°C

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.014

activity in organelles, cofactor NAD+, deamination of L-tryptophan

0.0155

activity in organelles, cofactor NADP+, deamination of L-tryptophan

0.0359

activity in organelles, cofactor NADH, amination of L-tryptophan

0.648

activity in organelles, cofactor NADPH, amination of L-tryptophan

0.87

cofactor NADH, activity in normal BV-N strain

1.22

cofactor NADPH, activity in normal BV-N strain

1.24

cofactor NADH or NADPH, activity in tumor tobacco tissue strains T-24

1.57

cofactor NADH, activity in tumor tobacco tissue strain C-58

1.59

cofactor NADPH, activity in tumor tobacco tissue strain C-58

activity in the apical part of the epicotyl in five-day-old etiolated seedlings 48 h after root excision

391540

activity in the apical part of the epicotyl in five-day-old etiolated seedlings immidiately after root excision

391540

activity in roots, cofactor NADH

activity in the apical part of the epicotyl in five-day-old etiolated seedlings 12 h after root excision

391540

activity in shoots, cofactor NADH

activity in roots, cofactor NADPH

activity in shoots, cofactor NADPH

activity in shoots, cofactor NADH

activity in shoots, cofactor NADH

activity in shoots, cofactor NADH

activity in shoots, cofactor NADPH

activity in shoots, cofactor NADPH

activity in shoots, cofactor NADPH

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

for deamination of L-tryptophan

7.5

show all columns Go to Temperature Optimum Search

for amination of 3-indolpyruvate

8.5

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at room temperature

assay at room temperature

assay at room temperature

assay at room temperature

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TEMPERATURE RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

35 - 55

more than 50% activity between 35 and 55°C

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

normal and crown-gall tumor tissue cultures, tissue transformed by Agrobacterium tumefaciens

brenda

no activity in Brassica oleracea

2 entries

3 entries

UniProt

brenda

2 entries

pea

391537, 391539, 391540

brenda

brenda

tomato

brenda

spinach

brenda

maize

brenda

no activity in Brassica oleracea

brenda

no activity in Brassica oleracea

kohlrabi

brenda

UniProt

brenda

brenda

UniProt

brenda

UniProt

brenda

brenda