Information on EC 1.5.1.23 - Tauropine dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.1.23
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RECOMMENDED NAME
GeneOntology No.
Tauropine dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tauropine + NAD+ + H2O = taurine + pyruvate + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyruvate fermentation to opines
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SYSTEMATIC NAME
IUBMB Comments
N2-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming)
In the reverse reaction, alanine can act instead of taurine, but more slowly, and 2-oxobutanoate and 2-oxopentanoate can act instead of pyruvate.
CAS REGISTRY NUMBER
COMMENTARY hide
104645-74-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
Anthopleura pacifica
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Balanus cariosus
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Amphitrite sp.
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Manually annotated by BRENDA team
no activity in Aplysia juliana
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Manually annotated by BRENDA team
no activity in Aplysia kurodai
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Manually annotated by BRENDA team
no activity in Aurelia aurita
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Manually annotated by BRENDA team
no activity in Bugula neritina
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Manually annotated by BRENDA team
no activity in Cerebratulus sp.
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Manually annotated by BRENDA team
no activity in Chaetopleura apiculata
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Manually annotated by BRENDA team
no activity in Chaetopterus variopedatus
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Manually annotated by BRENDA team
no activity in Clymenella torquata
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Manually annotated by BRENDA team
no activity in Crassostrea virginica
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Manually annotated by BRENDA team
no activity in Crepidula fornicata
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Manually annotated by BRENDA team
no activity in Dentalium pilsbryi
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Manually annotated by BRENDA team
no activity in Glycera sp.
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Manually annotated by BRENDA team
no activity in Halocynthia roretzi
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Manually annotated by BRENDA team
no activity in Hemigrapsus sanguineus
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Manually annotated by BRENDA team
no activity in Hexagrammos otakii
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Manually annotated by BRENDA team
no activity in Hydroides sp.
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Manually annotated by BRENDA team
no activity in Lepidonotus sp.
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Manually annotated by BRENDA team
no activity in Lineus sp.
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Manually annotated by BRENDA team
no activity in Littorina littorea
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Manually annotated by BRENDA team
no activity in Loligo bleekeri
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Manually annotated by BRENDA team
no activity in Lyonsia hyalina
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Manually annotated by BRENDA team
no activity in Membranipora tenuis
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Manually annotated by BRENDA team
no activity in Mopalia muscosa
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Manually annotated by BRENDA team
no activity in Mya arenaria
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Manually annotated by BRENDA team
no activity in Mytilus edulis
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Manually annotated by BRENDA team
no activity in Nereis sp.
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Manually annotated by BRENDA team
no activity in Nucella lapillus
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Manually annotated by BRENDA team
no activity in Nucula proxima
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Manually annotated by BRENDA team
no activity in Octopus membranaceus
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Manually annotated by BRENDA team
no activity in Oncorhynchus keta
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Manually annotated by BRENDA team
no activity in Phascolopsis sp.
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Manually annotated by BRENDA team
no activity in Phascolosoma sp.
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Manually annotated by BRENDA team
no activity in Phoronis architecta
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Manually annotated by BRENDA team
no activity in Phoronis vancouverensis
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Manually annotated by BRENDA team
no activity in Priapulus sp.
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Manually annotated by BRENDA team
no activity in Pseudocardium sachalinensis
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Manually annotated by BRENDA team
no activity in Pugettia quadridens
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Manually annotated by BRENDA team
no activity in Schizoporella floridana
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Manually annotated by BRENDA team
no activity in Solemya velum
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Manually annotated by BRENDA team
no activity in Spisula solidissima
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Manually annotated by BRENDA team
no activity in Stichopus japonicus
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Manually annotated by BRENDA team
no activity in Strongylocentrotus nudus
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Manually annotated by BRENDA team
no activity in Themiste sp.
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Manually annotated by BRENDA team
no activity in Urechis sp.
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Manually annotated by BRENDA team
no activity in Urosalpinx cinerea
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Rhodoglossum japonicum
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
; demosponge
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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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
Ala + pyruvate + NADH
?
show the reaction diagram
Aminomethane sulfonic acid + pyruvate + NADH
N2-(1-Carboxyethyl)aminomethanesulfonic acid + NAD+ + H2O
show the reaction diagram
Gly + pyruvate + NADH
?
show the reaction diagram
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at 6.7% of the activity with taurine
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Homotaurine + pyruvate + NADH
?
show the reaction diagram
Hypotaurine + pyruvate + NADH
N2-(1-Carboxyethyl)aminoethanesulfinic acid + NAD+ + H2O
show the reaction diagram
Taurine + 2-oxobutanoate + NADH
?
show the reaction diagram
Taurine + 2-oxohexanoate + NADH
?
show the reaction diagram
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at 4.8% of the activity with pyruvate
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Taurine + 2-oxopentanoate + NADH
?
show the reaction diagram
Taurine + 3-hydroxypyruvate + NADH
?
show the reaction diagram
Taurine + glyoxylate + NADH
?
show the reaction diagram
taurine + NADH + H+ + pyruvate
tauropine + NAD+ + H2O
show the reaction diagram
taurine is involved in osmoregulation in marine animals
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-
?
taurine + oxaloacetate + NADH
?
show the reaction diagram
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
show the reaction diagram
tauropine + NAD+ + H2O
taurine + pyruvate + NADH
show the reaction diagram
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r
Val + pyruvate + NADH
?
show the reaction diagram
Rhodoglossum japonicum
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at 17% of the activity with taurine
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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
taurine + NADH + H+ + pyruvate
tauropine + NAD+ + H2O
show the reaction diagram
B1GT63
taurine is involved in osmoregulation in marine animals
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?
tauropine + NAD+ + H2O
taurine + pyruvate + NADH
show the reaction diagram
Q8T882
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r
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
TaDH displays the GxGxxG/A motif known to be conserved among NAD(P)-dependent dehydrogenases
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxobutanoate
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slight substrate inhibition
5,5'-dithiobis(2-nitrobenzoate)
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sulfhydryl reagents restore activity
Fluorescein mercuric acetate
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sulfhydryl reagents restore activity
L-lactate
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competitive with respect to pyruvate
oxaloacetate
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slight substrate inhibition
pyruvate
succinate
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noncompetitive with respect to taurine and pyruvate
tauropine
additional information
level of expression of TaDH is controlled by oxygen: TaDH is expressed when the oxygen level is low, during anaerobic glycolysis
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.3 - 21.1
2-oxobutanoate
3.6
2-oxovalerate
0.051 - 0.29
NAD+
0.022 - 0.071
NADH
4.9
oxaloacetate
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-
0.068 - 0.8
pyruvate
15 - 44.4
taurine
0.39 - 30
tauropine
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
Rhodoglossum japonicum
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additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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tauropine formation
6.6 - 7.3
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tauropine formation, enzyme form TaDH-1
6.8
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tauropine formation
8.5
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tauropine oxidation
8.7 - 9.2
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tauropone oxidation
9
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tauropine oxidation
9.7
Rhodoglossum japonicum
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tauropine oxidation
10
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tauropine oxidation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1 - 7.2
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50% of maximal activity at pH 5.1 and at pH 7.2, tauropine formation
5.5 - 7.9
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50% of maximal activity at pH 5.5 and at pH 7.9, tauropine formation, enzyme form TaDH-1
5.5 - 7.4
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50% of maximal activity at pH 5.5 and at pH 7.4, tauropine formation
6.8 - 8.5
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50% of maximal activity at pH 6.8, optimum at pH 8.5, tauropine oxidation, enzyme form TaDH-1
8 - 9
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pH 8.0: 50% of maximal activity, pH 9.0: optimum, tauropine oxidation
8.7 - 9.2
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50% of maximal activity at pH 8.7 and at pH 9.2, tauropine oxidation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
theoretical value
5.44
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
sponges are collected in Croatia and whole bodys are used for enzyme characterization, high levels of this enzyme in most of cell types
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36920
calculated from amino acid sequence; deduced from cDNA and determined by SDS polyacrylamide gele electrophoresis and Western blot analysis
37000
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1 * 37000, SDS-PAGE
38000
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gel filtration
39000
Rhodoglossum japonicum
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gel filtration
41300
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1 * 41300, SDS-PAGE
42400
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gel filtration
43086
x * 43086, isozyme 1, amino acid sequence calculation, x * 43098, isozyme 2, amino acid sequence calculation, x * 43500, both isozymes, SDS-PAGE
43098
x * 43086, isozyme 1, amino acid sequence calculation, x * 43098, isozyme 2, amino acid sequence calculation, x * 43500, both isozymes, SDS-PAGE
43700
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43086, isozyme 1, amino acid sequence calculation, x * 43098, isozyme 2, amino acid sequence calculation, x * 43500, both isozymes, SDS-PAGE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
enzyme contains 2 possible N-glycoslyation sites but no carbohydrates
additional information
protein sequence contains a N-acetylated N-terminal serine and no intrachain disulfide bond
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
Rhodoglossum japonicum
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unstable above
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable to freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 2 mM KH2PO4-NaOH, pH 7.2, 1 mM EDTA, 10 mM 2-mercaptoethanol, stable for at least 3 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 enzyme forms: TaDH-1 and TaDH-2
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Ni-NTA-column chromatography; purification by metal-chelate affinity chromatography on a Ni-NTA-column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of the cDNA by PCR. DNA encoding TaDH is amplified by PCR from Suberites domuncula cDNA library, using the primers that are designed to amplify the complete open reading frame. Expression in Escherichia coli as His-tag fusion protein. Two allelic variants are identified, which are present in the different specimens either in a homozygotic or in a heterozygotic way (length polymorphism (453 bp and 468 bp long) is detected in the second intron and the beginning of third exon).
DNA and amino acid sequence determination and analysis, sequence comparisons