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(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
L-phenylalanine + NAD+ + H2O
phenylpyruvate + NH3 + NADH + H+
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
additional information
?
-
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
-
-
-
-
r
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
-
-
-
-
r
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
-
-
-
r
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
-
-
-
r
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
-
-
-
-
r
L-phenylalanine + NAD+ + H2O
phenylpyruvate + NH3 + NADH + H+
-
23% activity compared to L-tryptophan
-
-
?
L-phenylalanine + NAD+ + H2O
phenylpyruvate + NH3 + NADH + H+
-
23% activity compared to L-tryptophan
-
-
?
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
-
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
no activity with D-tryptophan
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
amination proceeds more intensively than deamination
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
no activity with D-tryptophan
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
no activity with D-tryptophan
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
amination proceeds more intensively than deamination
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
no activity with D-tryptophan
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
amination proceeds more intensively than deamination
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
-
-
-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
-
the enzyme is highly specific for the deamination of amino acid L-tryptophan
-
-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
-
-
-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
-
the enzyme is highly specific for the deamination of amino acid L-tryptophan
-
-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
-
-
-
r
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
-
-
-
-
r
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
-
-
-
r
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
-
-
-
r
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
-
-
-
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
-
primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
-
-
-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
-
the enzyme is highly specific for the deamination of amino acid L-tryptophan
-
-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
-
-
-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
-
the enzyme is highly specific for the deamination of amino acid L-tryptophan
-
-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.014
(indol-3-yl)pyruvate
-
at pH 7.5 and 25°C
0.025
NAD+
-
at pH 11.0 and 25°C
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
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16
(indol-3-yl)pyruvate
-
at pH 7.5 and 25°C
4.3
NAD+
-
at pH 11.0 and 25°C
21
NADH
-
at pH 7.5 and 25°C
17
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
8
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
10
L-tryptophan
mutant enzyme I296A, at pH 11.0 and 25°C
12
L-tryptophan
mutant enzyme M40L, at pH 11.0 and 25°C
20
L-tryptophan
wild type enzyme, at pH 11.0 and 25°C
21
L-tryptophan
mutant enzyme Y292F, at pH 11.0 and 25°C
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1100
(indol-3-yl)pyruvate
-
at pH 7.5 and 25°C
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
62
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
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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
14
-
activity in the apical part of the epicotyl in five-day-old etiolated seedlings 48 h after root excision
18
-
activity in the apical part of the epicotyl in five-day-old etiolated seedlings immidiately after root excision
22
-
activity in roots, cofactor NADH
23
-
activity in the apical part of the epicotyl in five-day-old etiolated seedlings 12 h after root excision
28
-
activity in shoots, cofactor NADH
30
-
activity in roots, cofactor NADPH
39
-
activity in shoots, cofactor NADPH
45
-
activity in shoots, cofactor NADH
52
-
activity in shoots, cofactor NADH
6
-
activity in shoots, cofactor NADH
64
-
activity in shoots, cofactor NADPH
70
-
activity in shoots, cofactor NADPH
9
-
activity in shoots, cofactor NADPH
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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A234D
the mutant shows higher specific activity and stability compared to the wild type enzyme
A69L
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
A69M
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
D168G
the mutant shows higher specific activity and stability compared to the wild type enzyme
I296A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I296N
the mutant shows wild type specific activity and higher stability compared to the wild type enzyme
L288M
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
L59F
the mutant shows higher specific activity and stability compared to the wild type enzyme
M295A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
M40L
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
M65A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
V132A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
V133A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
V291A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y292F
the mutant shows increased catalytic efficiency compared to the wild type enzyme
Y292H
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y292W
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
A234D
-
the mutant shows higher specific activity and stability compared to the wild type enzyme
-
D168G
-
the mutant shows higher specific activity and stability compared to the wild type enzyme
-
I296N
-
the mutant shows wild type specific activity and higher stability compared to the wild type enzyme
-
L59F
-
the mutant shows higher specific activity and stability compared to the wild type enzyme
-
L59F/D168G/A234D/I296N
-
mutant with thermal stability whose specific activity and stability are higher than those of the wild type enzyme
-
A69L
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
A69M
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
V132A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
V291A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
Y292F
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
-
L59F/D168G/A234D/I296N
mutant with thermal stability whose specific activity and stability are higher than those of the wild type enzyme
L59F/D168G/A234D/I296N
the mutant exhibits higher stability and specific activity than the wild type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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El Bahr, M.K.; Kutacek, M.; Opatrny, Z.
L-tryptophan aminotransferase and L-tryptophan dehydrogenase, enzymes of IAA synthesis, in normal and tumorous tobacco tissue cultures
Biochem. Physiol. Pflanz.
182
213-222
1987
Nicotiana tabacum
-
brenda
Kutacek, M.
Auxin biosynthesis and its regulation on the molecular level
Biol. Plant.
27
145-153
1985
Solanum lycopersicum, no activity in Brassica oleracea, Pisum sativum, Zea mays
-
brenda
Vackova, K.; Mehta, A.; Kutacek, M.
Tryptophan aminotransferase and tryptophan dehydrogenase activities in some cell compartments of spinach leaves: the effect of calcium ions on tryptophan dehydrogenase
Biol. Plant.
27
154-158
1985
Spinacia oleracea
-
brenda
Ebeid, M.M.; Dimova, S.; Kutacek, M.
Substrate specificity of L-tryptophan dehydrogenase and its distribution in plants
Biol. Plant.
27
413-416
1985
Solanum lycopersicum, no activity in Brassica oleracea, Pisum sativum, Prosopis juliflora, Zea mays
-
brenda
Tan Hoang Minh, M.; Kutacek, M.; Sebanek, J.
Growth-correlative effect of the root on the apical part of the epicotyl in pea seedlings regarding the IAA content and L-tryptophan aminotransferase and L-tryptophan dehydrogenase activities
Biol. Plant.
26
342-348
1984
Pisum sativum
-
brenda
Wakamatsu, T.; Sakuraba, H.; Kitamura, M.; Hakumai, Y.; Fukui, K.; Ohnishi, K.; Ashiuchi, M.; Ohshima, T.
Structural insights into l-tryptophan dehydrogenase from a photoautotrophic Cyanobacterium, Nostoc punctiforme
Appl. Environ. Microbiol.
83
e02710
2017
Nostoc punctiforme (W8CV45), Nostoc punctiforme, Nostoc punctiforme NIES-2108 (W8CV45), Nostoc punctiforme NIES-2108
brenda
Ogura, R.; Wakamatsu, T.; Mutaguchi, Y.; Doi, K.; Ohshima, T.
Biochemical characterization of an L-tryptophan dehydrogenase from the photoautotrophic cyanobacterium Nostoc punctiforme
Enzyme Microb. Technol.
60
40-46
2014
Nostoc punctiforme, Nostoc punctiforme NIES-2108
brenda
Matsui, D.; Okazaki, S.; Matsuda, M.; Asano, Y.
Enhancement of stability of L-tryptophan dehydrogenase from Nostoc punctiforme ATCC29133 and its application to L-tryptophan assay
J. Biotechnol.
196-197
27-32
2015
Nostoc punctiforme (W8CV45), Nostoc punctiforme ATCC29133 (W8CV45), Nostoc punctiforme ATCC29133
brenda