Information on EC 1.4.1.19 - tryptophan dehydrogenase

for references in articles please use BRENDA:EC1.4.1.19
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.4.1.19
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RECOMMENDED NAME
GeneOntology No.
tryptophan dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + NAD(P)+ + H2O = (indol-3-yl)pyruvate + NH3 + NAD(P)H + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
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Deamination
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-
-
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oxidation
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-
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:NAD(P)+ oxidoreductase (deaminating)
Activated by Ca2+.
CAS REGISTRY NUMBER
COMMENTARY hide
94047-13-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
normal and crown-gall tumor tissue cultures, tissue transformed by Agrobacterium tumefaciens
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Manually annotated by BRENDA team
no activity in Brassica oleracea
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Manually annotated by BRENDA team
tomato
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Manually annotated by BRENDA team
spinach
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Manually annotated by BRENDA team
maize
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
show the reaction diagram
L-phenylalanine + NAD+ + H2O
phenylpyruvate + NH3 + NADH + H+
show the reaction diagram
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
show the reaction diagram
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
show the reaction diagram
L-tryptophan + NAD(P)+
indol-3-yl-pyruvate + NH3 + NAD(P)H
show the reaction diagram
L-tryptophan + NAD+ + H2O
(indol-3-yl)pyruvate + NH3 + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
NAD(P)H
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(indol-3-yl)pyruvate
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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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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not influenced by EDTA (10 mM), KCl (100 mM) or DMSO (1% (v/v))
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014
(indol-3-yl)pyruvate
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at pH 7.5 and 25C
0.017 - 1.1
L-tryptophan
0.025
NAD+
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at pH 11.0 and 25C
0.038 - 1.46
NADH
130
NH3
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at pH 7.5 and 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16
(indol-3-yl)pyruvate
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at pH 7.5 and 25C
0.39 - 21
L-tryptophan
4.3
NAD+
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at pH 11.0 and 25C
21
NADH
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at pH 7.5 and 25C
17
NH3
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at pH 7.5 and 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1100
(indol-3-yl)pyruvate
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at pH 7.5 and 25C
0.75 - 540
L-tryptophan
170
NAD+
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at pH 11.0 and 25C
550
NADH
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at pH 7.5 and 25C
0.13
NH3
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at pH 7.5 and 25C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014
(indol-3-yl)pyruvate
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at pH 11.0 and 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.014
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activity in organelles, cofactor NAD+, deamination of L-tryptophan
0.0155
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activity in organelles, cofactor NADP+, deamination of L-tryptophan
0.0359
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activity in organelles, cofactor NADH, amination of L-tryptophan
0.648
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activity in organelles, cofactor NADPH, amination of L-tryptophan
0.87
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cofactor NADH, activity in normal BV-N strain
1.22
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cofactor NADPH, activity in normal BV-N strain
1.24
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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
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cofactor NADPH, activity in tumor tobacco tissue strain C-58
6
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activity in shoots, cofactor NADH
9
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activity in shoots, cofactor NADPH
14
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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
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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
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activity in shoots, cofactor NADH
30
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activity in roots, cofactor NADPH
39
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activity in shoots, cofactor NADPH
45
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activity in shoots, cofactor NADH
52
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activity in shoots, cofactor NADH
64
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activity in shoots, cofactor NADPH
70
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activity in shoots, cofactor NADPH
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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for amination of 3-indolpyruvate
11
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for deamination of L-tryptophan
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 55
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more than 50% activity between 35 and 55C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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normal and crown-gall tumor tissue cultures, tissue transformed by Agrobacterium tumefaciens
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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enzyme occurs in cytoplasm, chloroplast and pellet of remaining organelles sedimenting at 97000 * g
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
76100
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11.5
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the enzyme retains more than 80% of its activity after incubation for 30 min at pH 5.0 to 11.5
742410
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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the enzyme retains 19.3% activity after incubation at 4C for 24 h
40 - 50
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the enzyme retains full activity after incubation for 10 min at temperatures up to 40C. There is a complete loss of activity when the enzyme is incubated at temperatures above 50C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
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Ni-NTA column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli JM109 cells
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expressed in Escherichia coli Rosetta-gami2(DE3)pLysS cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A234D
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the mutant shows higher specific activity and stability compared to the wild type enzyme
A69L
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
A69M
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
D168G
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the mutant shows higher specific activity and stability compared to the wild type enzyme
I296A
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I296N
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the mutant shows wild type specific activity and higher stability compared to the wild type enzyme
L288M
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
L59F
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the mutant shows higher specific activity and stability compared to the wild type enzyme
L59F/D168G/A234D/I296N
M295A
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
M40L
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
M65A
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
V132A
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
V133A
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
V291A
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y292F
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the mutant shows increased catalytic efficiency compared to the wild type enzyme
Y292H
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y292W
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
A234D
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the mutant shows higher specific activity and stability compared to the wild type enzyme
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D168G
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the mutant shows higher specific activity and stability compared to the wild type enzyme
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I296N
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the mutant shows wild type specific activity and higher stability compared to the wild type enzyme
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L59F
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the mutant shows higher specific activity and stability compared to the wild type enzyme
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L59F/D168G/A234D/I296N
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mutant with thermal stability whose specific activity and stability are higher than those of the wild type enzyme
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A69L
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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A69M
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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V132A
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
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V291A
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
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Y292F
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the mutant shows increased catalytic efficiency compared to the wild type enzyme
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