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Information on EC 1.4.1.19 - tryptophan dehydrogenase for references in articles please use BRENDA:EC1.4.1.19Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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L-tryptophan + NAD(P)+ + H2O = (indol-3-yl)pyruvate + NH3 + NAD(P)H + H+
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L-tryptophan:NAD(P)+ oxidoreductase (deaminating)
Activated by Ca2+.
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dehydrogenase, tryptophan
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-
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-
L-Trp-dehydrogenase
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-
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-
L-tryptophan dehydrogenase
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-
-
-
NAD(P)-L-tryptophan dehydrogenase
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NAD+-dependent L-tryptophan dehydrogenase
L-Trp dehydrogenase
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NAD+-dependent L-tryptophan dehydrogenase
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NAD+-dependent L-tryptophan dehydrogenase
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NAD+-dependent L-tryptophan dehydrogenase
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NAD+-dependent L-tryptophan dehydrogenase
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TrpDH
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normal and crown-gall tumor tissue cultures, tissue transformed by Agrobacterium tumefaciens
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brenda
no activity in Brassica oleracea
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UniProt
brenda
pea
-
-
brenda
-
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-
brenda
tomato
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brenda
spinach
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brenda
maize
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brenda
no activity in Brassica oleracea
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brenda
no activity in Brassica oleracea
kohlrabi
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-
brenda
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UniProt
brenda
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brenda
-
UniProt
brenda
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brenda
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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
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(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
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-
-
r
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
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-
-
r
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
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-
-
-
r
L-phenylalanine + NAD+ + H2O
phenylpyruvate + NH3 + NADH + H+
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23% activity compared to L-tryptophan
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-
?
L-phenylalanine + NAD+ + H2O
phenylpyruvate + NH3 + NADH + H+
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23% activity compared to L-tryptophan
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-
?
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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-
-
r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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no activity with D-tryptophan
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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amination proceeds more intensively than deamination
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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no activity with D-tryptophan
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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no activity with D-tryptophan
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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amination proceeds more intensively than deamination
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
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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
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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no activity with D-tryptophan
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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amination proceeds more intensively than deamination
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
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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
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r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
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-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
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r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
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the enzyme is highly specific for the deamination of amino acid L-tryptophan
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r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
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r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
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the enzyme is highly specific for the deamination of amino acid L-tryptophan
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r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
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-
r
additional information
?
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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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additional information
?
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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
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r
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
W8CV45
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r
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
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r
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
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primary enzyme of indolylpyruvate pathway leading to indol-3-yl-acetic acid in plants, metabolism of indole compounds in plants
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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+
W8CV45
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-
-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
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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
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-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
W8CV45
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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
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-
r
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
W8CV45
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-
-
r
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NAD(P)+
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NAD(P)H
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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(P)H
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effect of NADPH compared to NADH is distinctly higher
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Ca2+
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Ca2+
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optimal activation at 0.8 mM
additional information
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the enzyme is not activated by metal ions
additional information
-
absence of heavy metal ions in active centre
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(indol-3-yl)pyruvate
-
substrate inhibition
EDTA
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reactivation by Ca2+ and Mn2+
additional information
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presence of a carbonyl group in the active centre, less sensitive to SH-inhibitors than glutamate dehydrogenase
-
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additional information
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not influenced by EDTA (10 mM), KCl (100 mM) or DMSO (1% (v/v))
-
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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; mutant enzyme M40L, at pH 11.0 and 25°C; 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
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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; 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
-
mutant enzyme V133A, at pH 11.0 and 25°C
140
L-tryptophan
-
at pH 11.0 and 25°C
170
L-tryptophan
-
mutant enzyme I296A, at pH 11.0 and 25°C; mutant enzyme M295A, at pH 11.0 and 25°C; 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
(indol-3-yl)pyruvate
-
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
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cofactor NADH, activity in tumor tobacco tissue strain C-58
1.59
-
cofactor NADPH, activity in tumor tobacco tissue strain C-58
6
-
activity in shoots, cofactor NADH
9
-
activity in shoots, cofactor NADPH
14
-
activity in the apical part of the epicotyl in five-day-old etiolated seedlings 48 h after root excision
18
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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
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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
64
-
activity in shoots, cofactor NADPH
70
-
activity in shoots, cofactor NADPH
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7.5
-
for amination of 3-indolpyruvate
11
-
for deamination of L-tryptophan
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22
-
assay at room temperature
22
-
assay at room temperature
22
-
assay at room temperature
22
-
assay at room temperature
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35 - 55
-
more than 50% activity between 35 and 55°C
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-
brenda
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normal and crown-gall tumor tissue cultures, tissue transformed by Agrobacterium tumefaciens
brenda
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brenda
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-
brenda
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-
brenda
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-
brenda
-
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brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
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-
-
brenda
-
-
brenda
additional information
-
enzyme occurs in cytoplasm, chloroplast and pellet of remaining organelles sedimenting at 97000 * g
-
brenda
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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.
?
-
x * 40000, SDS-PAGE
?
-
x * 40000, SDS-PAGE
-
homodimer
-
2 * 40000, SDS-PAGE
homodimer
-
2 * 39500, calculated from amino acid sequence
homodimer
-
2 * 39500, calculated from amino acid sequence; 2 * 40000, SDS-PAGE
-
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hanging drop vapor diffusion method, using 0.1 M HEPES-NaOH (pH 7.5), 14% (w/v) polyethylene glycol 8000, and 8% (v/v) ethylene glycol
-
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5 - 11.5
-
the enzyme retains more than 80% of its activity after incubation for 30 min at pH 5.0 to 11.5
742410
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4
-
the enzyme retains 19.3% activity after incubation at 4°C for 24 h
40 - 50
-
the enzyme retains full activity after incubation for 10 min at temperatures up to 40°C. There is a complete loss of activity when the enzyme is incubated at temperatures above 50°C
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Ni-NTA agarose column chromatography
-
Ni-NTA column chromatography
-
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expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli JM109 cells
-
expressed in Escherichia coli Rosetta-gami2(DE3)pLysS cells
-
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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
-
the mutant exhibits higher stability and specific activity than 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
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W8CV45_NOSPU
353
38472
TrEMBL
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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
no activity in Brassica oleracea, Pisum sativum, Solanum lycopersicum, 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
no activity in Brassica oleracea, Pisum sativum, Prosopis juliflora, Solanum lycopersicum, 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, Nostoc punctiforme (W8CV45), Nostoc punctiforme NIES-2108, Nostoc punctiforme NIES-2108 (W8CV45)
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, Nostoc punctiforme ATCC29133 (W8CV45)
brenda
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