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Information on EC 1.4.1.19 - tryptophan dehydrogenase
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1.4.1.19 tryptophan dehydrogenaseIUBMB Comments
Activated by Ca2+.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
dehydrogenase, tryptophan, L-Trp dehydrogenase, L-Trp-dehydrogenase, L-tryptophan dehydrogenase, NAD(P)-L-tryptophan dehydrogenase, NAD+-dependent L-tryptophan dehydrogenase, TDH, TrpDH, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, tryptophan
-
-
-
-
L-Trp dehydrogenase
L-Trp-dehydrogenase
-
-
-
-
L-tryptophan dehydrogenase
-
-
-
-
NAD(P)-L-tryptophan dehydrogenase
-
-
-
-
NAD+-dependent L-tryptophan dehydrogenase
TDH
-
-
-
-
TrpDH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + NAD(P)+ + H2O = (indol-3-yl)pyruvate + NH3 + NAD(P)H + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
-
-
-
-
Deamination
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:NAD(P)+ oxidoreductase (deaminating)
Activated by Ca2+.
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CAS REGISTRY NUMBER
COMMENTARY
94047-13-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
-
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+
-
-
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
-
-
-
-
r
(indol-3-yl)pyruvate + NH3 + NADH + H+
L-tryptophan + NAD+ + H2O
W8CV45
-
-
-
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+
W8CV45
-
-
-
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+
W8CV45
-
-
-
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+
W8CV45
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD(P)H
-
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
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
LITERATURE
IMAGE
additional information
-
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
LITERATURE
IMAGE
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
0.268
L-tryptophan
-
mutant enzyme L59F/D168G/A234D/I296N, at pH 11.5 and 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
L-tryptophan
-
mutant enzyme A69L, at pH 11.0 and 25°C; mutant enzyme A69M, at pH 11.0 and 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0155
-
activity in organelles, cofactor NADP+, deamination of L-tryptophan
1.24
-
cofactor NADH or NADPH, activity in tumor tobacco tissue strains T-24
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
23
-
activity in the apical part of the epicotyl in five-day-old etiolated seedlings 12 h after root excision
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
normal and crown-gall tumor tissue cultures, tissue transformed by Agrobacterium tumefaciens
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
enzyme occurs in cytoplasm, chloroplast and pellet of remaining organelles sedimenting at 97000 * g
-
brenda
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homodimer
-
2 * 39500, calculated from amino acid sequence; 2 * 40000, SDS-PAGE
-
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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
L59F/D168G/A234D/I296N
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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