BRENDA - Enzyme Database show
show all sequences of 1.1.1.103

Highly selective L-threonine 3-dehydrogenase from Cupriavidus necator and its use in determination of L-threonine

Ueatrongchit, T.; Asano, Y.; Anal. Biochem. 410, 44-56 (2011)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
14% activation at 10 mM
Cupriavidus necator
DTT
25% activation at 10 mM
Cupriavidus necator
Cloned(Commentary)
Commentary
Organism
DNA and amino acid seuence determination and analysis, sequence comparisons, phylogenetic tree, expression of His-tagged enzyme in Escherichia coli strains JM109 and BL21(DE3)
Cupriavidus necator
Inhibitors
Inhibitors
Commentary
Organism
Structure
4-chloromercuribenzonic acid
94% inhibition at 10 mM
Cupriavidus necator
calcium pantothenate
slight inhibition
Cupriavidus necator
FeCl2
32% inhibition at 1 mM after 60 min
Cupriavidus necator
FeCl3
73% inhibition at 1 mM after 60 min
Cupriavidus necator
HgCl2
77% inhibition at 1 mM after 60 min
Cupriavidus necator
iodoacetamide
99% inhibition at 10 mM
Cupriavidus necator
iodoacetic acid
52% inhibition at 10 mM
Cupriavidus necator
K3[Fe(CN)6]
25% inhibition at 10 mM
Cupriavidus necator
additional information
poor inhibition by K[Fe(CN)6], no inhibition by ethylene diamine tetraacetic acid and ethylene glycol tetraacetic acid, and by trypsin inhibitor T-9378
Cupriavidus necator
N-ethylmaleimide
complete inhibition
Cupriavidus necator
NaN3
88% inhibition at 10 mM
Cupriavidus necator
phenazinemethosulfate
complete inhibition
Cupriavidus necator
phenylmethanesulfonyl fluoride
63% inhibition at 10 mM
Cupriavidus necator
SnCl2
16% inhibition at 1 mM after 60 min
Cupriavidus necator
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.1
-
NAD+
pH 10.0, 30°C, native enzyme
Cupriavidus necator
11.6
-
L-threonine
pH 10.0, 30°C, native enzyme
Cupriavidus necator
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
AlCl3
18% activation at 1 mM
Cupriavidus necator
BaCl2
13% activation at 1 mM
Cupriavidus necator
CoCl2
15% activation at 1 mM
Cupriavidus necator
CrCl3
10% activation at 1 mM
Cupriavidus necator
CsCl
17% activation at 1 mM
Cupriavidus necator
CuSO4
15% activation at 1 mM
Cupriavidus necator
MgSO4
12% activation at 1 mM
Cupriavidus necator
MnSO4
12% activation at 1 mM
Cupriavidus necator
additional information
no effect at 1 mM by AgNO3, MgCl2, and 10 mM EDTA and ethylene glycol tetraacetic acid
Cupriavidus necator
Na2MoO4
13% activation at 1 mM
Cupriavidus necator
NiCl2
19% activation at 1 mM
Cupriavidus necator
PbCl2
18% activation at 1 mM
Cupriavidus necator
ZnSO4
9% activation at 1 mM
Cupriavidus necator
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34628
-
2 x 37200, native enzyme, SDS-PAGE, x * 34628, sequence calculation
Cupriavidus necator
79400
-
native enzyme, gel filtration
Cupriavidus necator
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-threonine + NAD+
Cupriavidus necator
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
?
L-threonine + NAD+
Cupriavidus necator NBRC 102504
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Cupriavidus necator
E5RQ20
-
-
Cupriavidus necator NBRC 102504
E5RQ20
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme 4.2fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, native enzyme 75.4fold by anion exchange and hydrophobic interaction chromatography, dialysis, hydroxyapatite chromatography, followed by gel filtration
Cupriavidus necator
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
42.2
-
purified native enzyme, pH 10.0, 30°C
Cupriavidus necator
65
-
purified recombinant enzyme, pH 10.0, 30°C
Cupriavidus necator
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
DL-2-amino-3-hydroxyvalerate + NAD+
-
721272
Cupriavidus necator
DL-2-amino-3-oxopentanoate + NADH + H+
-
-
-
?
DL-2-amino-3-hydroxyvalerate + NAD+
-
721272
Cupriavidus necator NBRC 102504
DL-2-amino-3-oxopentanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
-
721272
Cupriavidus necator
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
-
721272
Cupriavidus necator NBRC 102504
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
additional information
L-threonine and DL-2-amino-3-hydroxyvalerate are the only substrates for ThrDH among other L-amino acids, alcohols, and amino alcohols, substrate specificity, overview
721272
Cupriavidus necator
?
-
-
-
-
additional information
L-threonine and DL-2-amino-3-hydroxyvalerate are the only substrates for ThrDH among other L-amino acids, alcohols, and amino alcohols, substrate specificity, overview
721272
Cupriavidus necator NBRC 102504
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
2 x 37200, native enzyme, SDS-PAGE, x * 34628, sequence calculation
Cupriavidus necator
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
75
-
-
Cupriavidus necator
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
80
activity range, profile overview
Cupriavidus necator
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
25
75
quite stable at, rapid loss of activity above 80°C
Cupriavidus necator
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
38
-
NAD+
pH 10.0, 30°C, native enzyme
Cupriavidus necator
43.8
-
L-threonine
pH 10.0, 30°C, native enzyme
Cupriavidus necator
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
10
-
glycine-KOH buffer
Cupriavidus necator
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
12
activity range, pH-dependent activity varies in different buffer systems, profile overview
Cupriavidus necator
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
4
11
the purified enzyme is very stable from pH 6.0 to pH 11.0 in the glycine-KOH system, the enzyme is unstable in sodium acetate buffer, pH 4.0-5.0, and Na2CO3-NaHCO3 buffer, pH 10.0-11.0
Cupriavidus necator
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
dependent on
Cupriavidus necator
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
14% activation at 10 mM
Cupriavidus necator
DTT
25% activation at 10 mM
Cupriavidus necator
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid seuence determination and analysis, sequence comparisons, phylogenetic tree, expression of His-tagged enzyme in Escherichia coli strains JM109 and BL21(DE3)
Cupriavidus necator
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
dependent on
Cupriavidus necator
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
4-chloromercuribenzonic acid
94% inhibition at 10 mM
Cupriavidus necator
calcium pantothenate
slight inhibition
Cupriavidus necator
FeCl2
32% inhibition at 1 mM after 60 min
Cupriavidus necator
FeCl3
73% inhibition at 1 mM after 60 min
Cupriavidus necator
HgCl2
77% inhibition at 1 mM after 60 min
Cupriavidus necator
iodoacetamide
99% inhibition at 10 mM
Cupriavidus necator
iodoacetic acid
52% inhibition at 10 mM
Cupriavidus necator
K3[Fe(CN)6]
25% inhibition at 10 mM
Cupriavidus necator
additional information
poor inhibition by K[Fe(CN)6], no inhibition by ethylene diamine tetraacetic acid and ethylene glycol tetraacetic acid, and by trypsin inhibitor T-9378
Cupriavidus necator
N-ethylmaleimide
complete inhibition
Cupriavidus necator
NaN3
88% inhibition at 10 mM
Cupriavidus necator
phenazinemethosulfate
complete inhibition
Cupriavidus necator
phenylmethanesulfonyl fluoride
63% inhibition at 10 mM
Cupriavidus necator
SnCl2
16% inhibition at 1 mM after 60 min
Cupriavidus necator
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.1
-
NAD+
pH 10.0, 30°C, native enzyme
Cupriavidus necator
11.6
-
L-threonine
pH 10.0, 30°C, native enzyme
Cupriavidus necator
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
AlCl3
18% activation at 1 mM
Cupriavidus necator
BaCl2
13% activation at 1 mM
Cupriavidus necator
CoCl2
15% activation at 1 mM
Cupriavidus necator
CrCl3
10% activation at 1 mM
Cupriavidus necator
CsCl
17% activation at 1 mM
Cupriavidus necator
CuSO4
15% activation at 1 mM
Cupriavidus necator
MgSO4
12% activation at 1 mM
Cupriavidus necator
MnSO4
12% activation at 1 mM
Cupriavidus necator
additional information
no effect at 1 mM by AgNO3, MgCl2, and 10 mM EDTA and ethylene glycol tetraacetic acid
Cupriavidus necator
Na2MoO4
13% activation at 1 mM
Cupriavidus necator
NiCl2
19% activation at 1 mM
Cupriavidus necator
PbCl2
18% activation at 1 mM
Cupriavidus necator
ZnSO4
9% activation at 1 mM
Cupriavidus necator
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34628
-
2 x 37200, native enzyme, SDS-PAGE, x * 34628, sequence calculation
Cupriavidus necator
79400
-
native enzyme, gel filtration
Cupriavidus necator
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-threonine + NAD+
Cupriavidus necator
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
?
L-threonine + NAD+
Cupriavidus necator NBRC 102504
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme 4.2fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, native enzyme 75.4fold by anion exchange and hydrophobic interaction chromatography, dialysis, hydroxyapatite chromatography, followed by gel filtration
Cupriavidus necator
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
42.2
-
purified native enzyme, pH 10.0, 30°C
Cupriavidus necator
65
-
purified recombinant enzyme, pH 10.0, 30°C
Cupriavidus necator
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
DL-2-amino-3-hydroxyvalerate + NAD+
-
721272
Cupriavidus necator
DL-2-amino-3-oxopentanoate + NADH + H+
-
-
-
?
DL-2-amino-3-hydroxyvalerate + NAD+
-
721272
Cupriavidus necator NBRC 102504
DL-2-amino-3-oxopentanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
-
721272
Cupriavidus necator
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
-
721272
Cupriavidus necator NBRC 102504
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
additional information
L-threonine and DL-2-amino-3-hydroxyvalerate are the only substrates for ThrDH among other L-amino acids, alcohols, and amino alcohols, substrate specificity, overview
721272
Cupriavidus necator
?
-
-
-
-
additional information
L-threonine and DL-2-amino-3-hydroxyvalerate are the only substrates for ThrDH among other L-amino acids, alcohols, and amino alcohols, substrate specificity, overview
721272
Cupriavidus necator NBRC 102504
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 x 37200, native enzyme, SDS-PAGE, x * 34628, sequence calculation
Cupriavidus necator
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
75
-
-
Cupriavidus necator
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
80
activity range, profile overview
Cupriavidus necator
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
25
75
quite stable at, rapid loss of activity above 80°C
Cupriavidus necator
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
38
-
NAD+
pH 10.0, 30°C, native enzyme
Cupriavidus necator
43.8
-
L-threonine
pH 10.0, 30°C, native enzyme
Cupriavidus necator
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
10
-
glycine-KOH buffer
Cupriavidus necator
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
12
activity range, pH-dependent activity varies in different buffer systems, profile overview
Cupriavidus necator
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
4
11
the purified enzyme is very stable from pH 6.0 to pH 11.0 in the glycine-KOH system, the enzyme is unstable in sodium acetate buffer, pH 4.0-5.0, and Na2CO3-NaHCO3 buffer, pH 10.0-11.0
Cupriavidus necator
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to the extended short-chain alcohol dehydrogenase superfamily
Cupriavidus necator
additional information
the enzyme possesses a glycine-rich NAD+-binding domain at the N terminus and conserved catalytic triad of YxxxK residues
Cupriavidus necator
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to the extended short-chain alcohol dehydrogenase superfamily
Cupriavidus necator
additional information
the enzyme possesses a glycine-rich NAD+-binding domain at the N terminus and conserved catalytic triad of YxxxK residues
Cupriavidus necator
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
Structural insights on mouse L ...
Mus musculus
J. Struct. Biol.
192
510-518
2015
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1
1
5
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4
1
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737579
Lee
Effects of dietary levels of g ...
Gallus gallus
Asian-australas. J. Anim. Sci.
27
69-76
2014
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738606
Nakano
Binding of NAD+ and L-threonin ...
Cupriavidus necator
J. Biol. Chem.
289
10445-10454
2014
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738860
Ma
Identification and characteriz ...
Escherichia coli
J. Microbiol. Biotechnol.
24
748-755
2014
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11
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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
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722747
Yoneda
Crystal structure of binary an ...
Thermoplasma volcanium
J. Biol. Chem.
287
12966-12974
2012
1
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2
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1
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1
1
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1
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1
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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
-
-
-
14
2
-
13
2
2
-
8
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1
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-
2
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6
1
1
1
1
2
1
1
1
1
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1
1
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14
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13
2
2
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1
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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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Threonine metabolism in Japane ...
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Edgar
The human L-threonine 3-dehydr ...
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Investigation of a catalytic z ...
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Functional analysis of E. coli ...
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Purification and structural ch ...
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Mitochondrial L-threonine dehy ...
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Epperly
L-Threonine dehydrogenase from ...
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The sulfhydryl content of L-th ...
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1
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3
-
3
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1
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1
-
-
2
-
-
-
-
1
-
-
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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
-
2
-
1
-
3
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1
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1
-
1
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-
-
-
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1
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1
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5
-
4
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2
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1
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1
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1
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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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-
-
-
-
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1
2
-
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3
1
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2
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1
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2
1
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1
2
-
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-
1
1
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1
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-
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1
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1
-
2
-
-
3
1
-
-
-
1
-
2
1
-
1
2
-
-
-
-
1
1
-
-
-
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-
285716
Boylan
L-threonine dehydrogenase ...
Escherichia coli K-12
J. Biol. Chem.
256
1809-1815
1981
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-
-
-
-
-
5
2
-
1
1
1
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4
-
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1
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-
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1
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9
-
-
-
-
1
1
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1
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-
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-
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1
-
-
-
-
5
-
2
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1
1
1
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-
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1
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1
-
9
-
-
-
-
1
1
-
-
-
-
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-
-
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-
285717
Aoyama
L-Threonine dehydrogenase of c ...
Gallus gallus
J. Biol. Chem.
256
12367-12373
1981
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-
-
-
-
-
7
2
1
-
2
1
-
3
-
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1
-
-
2
1
1
1
1
-
-
-
-
1
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1
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1
-
-
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7
-
2
1
-
2
1
-
-
-
1
-
2
1
1
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
285718
Boylan
L-Threonine dehydrogenase of E ...
Escherichia coli K-12
Biochem. Biophys. Res. Commun.
85
190-197
1978
-
-
-
-
-
-
-
2
-
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1
1
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2
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1
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1
1
7
-
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1
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1
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1
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2
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1
1
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1
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1
1
7
-
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-
-
-
1
-
-
-
-
-
-
-
-
-
285719
McGilvray
-
L-Threonine dehydrogenase (Art ...
Arthrobacter sp.
Methods Enzymol.
17B
580-584
1971
-
-
-
-
-
1
4
2
-
3
-
1
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1
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1
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1
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1
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1
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1
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1
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1
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4
-
2
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3
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1
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1
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1
-
1
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1
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-
-
285720
Green
The enzymatic formation of ami ...
Gallus gallus, Oryctolagus cuniculus, Rattus norvegicus, Staphylococcus aureus, Sus scrofa
biochem. J.
92
537-548
1964
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-
-
-
-
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-
2
-
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5
-
5
-
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1
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7
1
-
5
-
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-
1
-
1
-
-
5
-
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-
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-
-
5
-
-
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2
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-
-
5
-
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1
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7
1
-
5
-
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-
1
-
1
-
-
-
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-
285721
Hartshorne
Studies on liver threonine deh ...
Rana catesbeiana
Arch. Biochem. Biophys.
105
173-178
1964
-
-
-
-
-
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4
2
-
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-
1
-
1
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1
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1
1
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1
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1
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1
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1
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4
-
2
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1
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1
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1
1
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1
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1
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