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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: Bacteria, Eukaryota
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
(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+
-
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
-
-
-
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
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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
0.268
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A6P1L140_9NOSO
353
0
38422
TrEMBL
other Location (Reliability: 2)
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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
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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
Y292F
the mutant shows increased catalytic efficiency compared to the wild type enzyme
V132A
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
L59F
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
V291A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
A69M
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
V133A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I296A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
L59F/D168G/A234D/I296N
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
L288M
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
Y292W
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y292H
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
M295A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D168G
the mutant shows higher specific activity and stability compared to the wild type enzyme
A234D
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
-
D168G
-
the mutant shows higher specific activity and stability compared to the wild type enzyme
-
A234D
-
the mutant shows higher specific activity and stability compared to the wild type enzyme
-
Y292F
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
-
V132A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
A69L
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
V291A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
A69M
-
the mutant shows severely reduced 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
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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
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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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
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
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