HOME
login
history
all enzymes
BRENDA home
History
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.
EC Tree
1.4.1.19 tryptophan dehydrogenaseIUBMB Comments
Activated by Ca2+.
Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
trpdh, l-tryptophan dehydrogenase, l-trp dehydrogenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + NAD(P)+ + H2O = (indol-3-yl)pyruvate + NH3 + NAD(P)H + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
-
-
-
-
Deamination
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:NAD(P)+ oxidoreductase (deaminating)
Activated by Ca2+.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
94047-13-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not influenced by EDTA (10 mM), KCl (100 mM) or DMSO (1% (v/v))
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
normal and crown-gall tumor tissue cultures, tissue transformed by Agrobacterium tumefaciens
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homodimer
-
2 * 39500, calculated from amino acid sequence; 2 * 40000, SDS-PAGE
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.4.1.19)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
