BRENDA - Enzyme Database show
show all sequences of 1.1.1.103

The first crystal structure of L-threonine dehydrogenase

Ishikawa, K.; Higashi, N.; Nakamura, T.; Matsuura, T.; Nakagawa, A.; J. Mol. Biol. 366, 857-867 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
orf PH0655, NA and amino acid sequence determination, analysis, and comparison, expression of selenomethionine-labeled wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Pyrococcus horikoshii
Crystallization (Commentary)
Crystallization
Organism
selenomethionine-substituted enzyme, 10 mg/ml protein in 50 mM Tris-HCl buffer, pH 7.5, hanging-drop vapor-diffusion method at 4°C, mixing of 0.0015 ml of each, protein and reservoir solution, the latter containing 0.2 M sodium chloride, 0.1 M HEPES buffer, pH 7.5, and 40% v/v PEG 400, five days, X-ray diffraction structure determination and analysis, single wavelength anomalous diffraction method
Pyrococcus horikoshii
Engineering
Amino acid exchange
Commentary
Organism
E199A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
Pyrococcus horikoshii
R204A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
Pyrococcus horikoshii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0099
-
NAD+
pH 7.5, 65°C, recombinant wild-type enzyme
Pyrococcus horikoshii
0.0118
-
L-threonine
pH 7.5, 65°C, recombinant wild-type enzyme
Pyrococcus horikoshii
0.291
-
NAD+
pH 7.5, 65°C, recombinant mutant R204A
Pyrococcus horikoshii
0.304
-
NAD+
pH 7.5, 65°C, recombinant mutant E199A
Pyrococcus horikoshii
1.51
-
L-threonine
pH 7.5, 65°C, recombinant mutant E199A
Pyrococcus horikoshii
2.5
-
L-threonine
pH 7.5, 65°C, recombinant mutant R204A
Pyrococcus horikoshii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
one molecule of TDH contains one zinc ion playing a structural role, the metal ion is ligated by foru Cys residues, coenzyme-binding domain shows a larger interdomain cleft compared to other ADHs, binding structure, overview
Pyrococcus horikoshii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
4 * 35000, recombinant enzyme, SDS-PAGE
Pyrococcus horikoshii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-threonine + NAD+
Pyrococcus horikoshii
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus horikoshii
O58389
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-threonine + NAD+
-
688343
Pyrococcus horikoshii
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
r
Subunits
Subunits
Commentary
Organism
More
crystal structure analysis, each subunit is composed of two domains: an NAD(H)-binding domain and a catalytic domain. The NAD(H)-binding domain contains the alpha/beta Rossmann fold motif, characteristic of the NAD(H)-binding protein
Pyrococcus horikoshii
tetramer
4 * 35000, recombinant enzyme, SDS-PAGE
Pyrococcus horikoshii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
65
-
assay at
Pyrococcus horikoshii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.55
-
L-threonine
pH 7.5, 65°C, recombinant mutant E199A
Pyrococcus horikoshii
0.55
-
NAD+
pH 7.5, 65°C, recombinant mutant E199A
Pyrococcus horikoshii
0.667
-
L-threonine
pH 7.5, 65°C, recombinant mutant R204A
Pyrococcus horikoshii
0.667
-
NAD+
pH 7.5, 65°C, recombinant mutant R204A
Pyrococcus horikoshii
11
-
L-threonine
pH 7.5, 65°C, recombinant wild-type enzyme
Pyrococcus horikoshii
11
-
NAD+
pH 7.5, 65°C, recombinant wild-type enzyme
Pyrococcus horikoshii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Pyrococcus horikoshii
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Pyrococcus horikoshii
NADH
-
Pyrococcus horikoshii
Cloned(Commentary) (protein specific)
Commentary
Organism
orf PH0655, NA and amino acid sequence determination, analysis, and comparison, expression of selenomethionine-labeled wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Pyrococcus horikoshii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Pyrococcus horikoshii
NADH
-
Pyrococcus horikoshii
Crystallization (Commentary) (protein specific)
Crystallization
Organism
selenomethionine-substituted enzyme, 10 mg/ml protein in 50 mM Tris-HCl buffer, pH 7.5, hanging-drop vapor-diffusion method at 4°C, mixing of 0.0015 ml of each, protein and reservoir solution, the latter containing 0.2 M sodium chloride, 0.1 M HEPES buffer, pH 7.5, and 40% v/v PEG 400, five days, X-ray diffraction structure determination and analysis, single wavelength anomalous diffraction method
Pyrococcus horikoshii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E199A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
Pyrococcus horikoshii
R204A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
Pyrococcus horikoshii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0099
-
NAD+
pH 7.5, 65°C, recombinant wild-type enzyme
Pyrococcus horikoshii
0.0118
-
L-threonine
pH 7.5, 65°C, recombinant wild-type enzyme
Pyrococcus horikoshii
0.291
-
NAD+
pH 7.5, 65°C, recombinant mutant R204A
Pyrococcus horikoshii
0.304
-
NAD+
pH 7.5, 65°C, recombinant mutant E199A
Pyrococcus horikoshii
1.51
-
L-threonine
pH 7.5, 65°C, recombinant mutant E199A
Pyrococcus horikoshii
2.5
-
L-threonine
pH 7.5, 65°C, recombinant mutant R204A
Pyrococcus horikoshii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
one molecule of TDH contains one zinc ion playing a structural role, the metal ion is ligated by foru Cys residues, coenzyme-binding domain shows a larger interdomain cleft compared to other ADHs, binding structure, overview
Pyrococcus horikoshii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
4 * 35000, recombinant enzyme, SDS-PAGE
Pyrococcus horikoshii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-threonine + NAD+
Pyrococcus horikoshii
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
r
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-threonine + NAD+
-
688343
Pyrococcus horikoshii
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
More
crystal structure analysis, each subunit is composed of two domains: an NAD(H)-binding domain and a catalytic domain. The NAD(H)-binding domain contains the alpha/beta Rossmann fold motif, characteristic of the NAD(H)-binding protein
Pyrococcus horikoshii
tetramer
4 * 35000, recombinant enzyme, SDS-PAGE
Pyrococcus horikoshii
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
65
-
assay at
Pyrococcus horikoshii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.55
-
L-threonine
pH 7.5, 65°C, recombinant mutant E199A
Pyrococcus horikoshii
0.55
-
NAD+
pH 7.5, 65°C, recombinant mutant E199A
Pyrococcus horikoshii
0.667
-
L-threonine
pH 7.5, 65°C, recombinant mutant R204A
Pyrococcus horikoshii
0.667
-
NAD+
pH 7.5, 65°C, recombinant mutant R204A
Pyrococcus horikoshii
11
-
L-threonine
pH 7.5, 65°C, recombinant wild-type enzyme
Pyrococcus horikoshii
11
-
NAD+
pH 7.5, 65°C, recombinant wild-type enzyme
Pyrococcus horikoshii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Pyrococcus horikoshii
Other publictions for EC 1.1.1.103
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738933
He
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1
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1
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738606
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Binding of NAD+ and L-threonin ...
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3
3
738860
Ma
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Escherichia coli
J. Microbiol. Biotechnol.
24
748-755
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1
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3
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4
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1
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11
1
1
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1
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1
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11
1
1
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-
1
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1
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-
723777
Han
Regulation of L-threonine dehy ...
Mus musculus
Stem Cells
31
953-965
2013
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2
2
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722747
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Thermoplasma volcanium
J. Biol. Chem.
287
12966-12974
2012
1
-
1
1
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2
2
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3
1
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5
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1
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1
1
1
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1
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1
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1
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1
1
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2
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2
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1
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1
1
1
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1
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1
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1
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1
1
-
-
-
721272
Ueatrongchit
Highly selective L-threonine 3 ...
Cupriavidus necator, Cupriavidus necator NBRC 102504
Anal. Biochem.
410
44-56
2011
2
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1
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14
2
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13
2
2
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8
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1
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2
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6
1
1
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1
2
1
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14
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2
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13
2
2
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1
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2
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6
1
1
1
1
2
1
1
1
-
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2
2
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-
698526
Bao
Biochemical characteristics an ...
Streptomyces sp. 139
J. Appl. Microbiol.
106
1140-1146
2009
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1
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1
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698673
Bashir
Highly thermostable L-threonin ...
Thermococcus kodakarensis KOD1
J. Biochem.
146
95-102
2009
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1
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1
2
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7
2
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1
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1
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699854
Bowyer
Structure and function of the ...
Thermococcus kodakarensis
J. Struct. Biol.
168
294-304
2009
-
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1
1
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1
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709827
Lee
Metabolic engineering of a red ...
Escherichia coli, Escherichia coli MDS42
Microb. Cell Fact.
8
02
2009
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710562
Wang
Dependence of mouse embryonic ...
Mus musculus
Science
325
435-439
2009
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687461
Higashi
Investigating a catalytic mech ...
Pyrococcus horikoshii
J. Biochem.
144
77-85
2008
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1
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7
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8
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1
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7
1
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1
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7
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8
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1
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1
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1
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1
1
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7
1
1
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695358
Bowyer
Crystallization and preliminar ...
Thermococcus kodakarensis
Acta Crystallogr. Sect. F
64
828-830
2008
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688343
Ishikawa
The first crystal structure of ...
Pyrococcus horikoshii
J. Mol. Biol.
366
857-867
2007
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1
1
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6
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1
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3
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1
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2
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668567
Machielsen
Production and characterizatio ...
Pyrococcus furiosus
FEBS J.
273
2722-2729
2006
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1
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Higashi
Crystallization and preliminar ...
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Acta crystallogr. Sect. F
61
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2005
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668111
Le Floch
Catabolism through the threoni ...
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Br. J. Nutr.
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2005
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668536
Shimizu
L-Threonine dehydrogenase from ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Extremophiles
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2005
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2
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10
1
1
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4
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1
1
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669546
Higashi
Kinetic study of thermostable ...
Pyrococcus horikoshii
J. Biosci. Bioeng.
99
175-180
2005
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1
1
1
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4
1
-
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654175
Akagi
Threonine metabolism in Japane ...
Coturnix japonica, Rattus norvegicus
Amino Acids
26
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2004
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2
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655857
Kazuoka
Novel psychrophilic and thermo ...
Cytophaga sp., Cytophaga sp. KUC-1
J. Bacteriol.
185
4483-4489
2003
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1
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1
12
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9
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5
1
12
1
1
1
3
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1
2
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655125
Edgar
Molecular cloning and tissue d ...
Mus musculus, Sus scrofa
BMC Biochem.
3
19
2002
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8
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2
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2
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655131
Edgar
The human L-threonine 3-dehydr ...
Homo sapiens
BMC Genet.
3
18
2002
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1
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285701
Yuan
Characterization of hepatic L- ...
Gallus gallus
Comp. Biochem. Physiol. B
130
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2001
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1
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1
1
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285702
Johnson
Investigation of a catalytic z ...
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Arch. Biochem. Biophys.
358
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1998
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2
1
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7
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7
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285703
Marcus
Identification of a second act ...
Escherichia coli K-12
Arch. Biochem. Biophys.
316
413-420
1995
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285704
Chen
Functional analysis of E. coli ...
Escherichia coli K-12
Biochim. Biophys. Acta
1253
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1995
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Wagner
Purification and characterizat ...
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1995
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8
1
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1
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285705
Kao
Purification and structural ch ...
Sus scrofa
Protein Expr. Purif.
5
423-431
1994
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1
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2
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1
1
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285706
Marcus
Threonine formation via the co ...
Escherichia coli K-12
J. Bacteriol.
175
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1993
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285707
Pagani
-
Mitochondrial L-threonine dehy ...
Rattus norvegicus
Biochem. Soc. Trans.
20
379
1992
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285708
Pagani
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Rat liver L-threonine dehydrog ...
Bos taurus, Rattus norvegicus
Biochem. Soc. Trans.
20
24
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3
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285709
Epperly
L-Threonine dehydrogenase from ...
Escherichia coli K-12
J. Biol. Chem.
266
6086-6092
1991
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285710
Craig
The sulfhydryl content of L-th ...
Escherichia coli K-12
Biochim. Biophys. Acta
1037
30-38
1990
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Aronson
The primary structure of Esche ...
Escherichia coli K-12
J. Biol. Chem.
264
5226-5232
1989
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285712
Craig
Cd2+ activation of L-threonine ...
Escherichia coli K-12
Biochim. Biophys. Acta
957
222-229
1988
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Tressel
Interaction between L-threonin ...
Sus scrofa
J. Biol. Chem.
261
16428-16437
1986
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285714
Craig
L-Threonine dehydrogenase from ...
Escherichia coli K-12
Biochemistry
25
1870-1876
1986
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5
4
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1
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285715
Ray
L-Threonine dehydrogenase from ...
Capra hircus
J. Biol. Chem.
260
5913-5918
1985
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2
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285716
Boylan
L-threonine dehydrogenase ...
Escherichia coli K-12
J. Biol. Chem.
256
1809-1815
1981
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2
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285717
Aoyama
L-Threonine dehydrogenase of c ...
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J. Biol. Chem.
256
12367-12373
1981
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2
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1
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285718
Boylan
L-Threonine dehydrogenase of E ...
Escherichia coli K-12
Biochem. Biophys. Res. Commun.
85
190-197
1978
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7
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1
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285719
McGilvray
-
L-Threonine dehydrogenase (Art ...
Arthrobacter sp.
Methods Enzymol.
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580-584
1971
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2
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285720
Green
The enzymatic formation of ami ...
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537-548
1964
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Hartshorne
Studies on liver threonine deh ...
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105
173-178
1964
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