BRENDA - Enzyme Database show
show all sequences of 1.1.1.103

Rat liver L-threonine dehydrogenase

Pagani, R.; Guerranti, R.; Right, S.; Leoncini, R.; Vannoni, D.; Marinello, E.; Biochem. Soc. Trans. 20, 24 (1991)
No PubMed abstract available

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-threonine + NAD+
Rattus norvegicus
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
Rattus norvegicus
-
L-threonine + NAD+
Bos taurus
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
Bos taurus
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bos taurus
-
-
-
Rattus norvegicus
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Bos taurus
-
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.032
-
enzyme activity in mitochondrial extracts prepared from fresh mitochondria
Rattus norvegicus
0.055
-
enzyme activity in mitochondrial extracts
Bos taurus
0.062
-
enzyme activity in mitochondrial extracts after freezing the mitochondria for 2 weeks at -20°C
Rattus norvegicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-threonine + NAD+
-
285708
Rattus norvegicus
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
285708
Rattus norvegicus
-
L-threonine + NAD+
-
285708
Bos taurus
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
285708
Bos taurus
-
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
crude enzyme extracts from mitochondria
Rattus norvegicus
9
-
crude enzyme extracts from mitochondria frozen for 14 days and dialyzed
Rattus norvegicus
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Bos taurus
NAD+
-
Rattus norvegicus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Bos taurus
NAD+
-
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-threonine + NAD+
Rattus norvegicus
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
Rattus norvegicus
-
L-threonine + NAD+
Bos taurus
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
Bos taurus
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Bos taurus
-
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.032
-
enzyme activity in mitochondrial extracts prepared from fresh mitochondria
Rattus norvegicus
0.055
-
enzyme activity in mitochondrial extracts
Bos taurus
0.062
-
enzyme activity in mitochondrial extracts after freezing the mitochondria for 2 weeks at -20°C
Rattus norvegicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-threonine + NAD+
-
285708
Rattus norvegicus
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
285708
Rattus norvegicus
-
L-threonine + NAD+
-
285708
Bos taurus
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
285708
Bos taurus
-
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
crude enzyme extracts from mitochondria
Rattus norvegicus
9
-
crude enzyme extracts from mitochondria frozen for 14 days and dialyzed
Rattus norvegicus
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)
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Binding of NAD+ and L-threonin ...
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Ma
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723777
Han
Regulation of L-threonine dehy ...
Mus musculus
Stem Cells
31
953-965
2013
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722747
Yoneda
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Thermoplasma volcanium
J. Biol. Chem.
287
12966-12974
2012
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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
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2
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698526
Bao
Biochemical characteristics an ...
Streptomyces sp. 139
J. Appl. Microbiol.
106
1140-1146
2009
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698673
Bashir
Highly thermostable L-threonin ...
Thermococcus kodakarensis KOD1
J. Biochem.
146
95-102
2009
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699854
Bowyer
Structure and function of the ...
Thermococcus kodakarensis
J. Struct. Biol.
168
294-304
2009
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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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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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668567
Machielsen
Production and characterizatio ...
Pyrococcus furiosus
FEBS J.
273
2722-2729
2006
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667071
Higashi
Crystallization and preliminar ...
Pyrococcus horikoshii
Acta crystallogr. Sect. F
61
432-434
2005
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668111
Le Floch
Catabolism through the threoni ...
Sus scrofa
Br. J. Nutr.
93
447-456
2005
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668536
Shimizu
L-Threonine dehydrogenase from ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Extremophiles
9
317-324
2005
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1
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3
3
2
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45
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1
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10
1
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4
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10
1
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4
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1
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669546
Higashi
Kinetic study of thermostable ...
Pyrococcus horikoshii
J. Biosci. Bioeng.
99
175-180
2005
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3
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2
1
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3
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4
1
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1
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1
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4
1
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654175
Akagi
Threonine metabolism in Japane ...
Coturnix japonica, Rattus norvegicus
Amino Acids
26
235-242
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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9
5
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2
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8
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1
1
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1
12
1
1
1
3
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4
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9
4
5
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1
12
1
1
1
3
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Molecular cloning and tissue d ...
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655131
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The human L-threonine 3-dehydr ...
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Characterization of hepatic L- ...
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285702
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Investigation of a catalytic z ...
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Identification of a second act ...
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285704
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Functional analysis of E. coli ...
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Purification and characterizat ...
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Kao
Purification and structural ch ...
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1994
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Threonine formation via the co ...
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Mitochondrial L-threonine dehy ...
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Rat liver L-threonine dehydrog ...
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Epperly
L-Threonine dehydrogenase from ...
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The sulfhydryl content of L-th ...
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1990
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The primary structure of Esche ...
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Craig
Cd2+ activation of L-threonine ...
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1988
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Interaction between L-threonin ...
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285714
Craig
L-Threonine dehydrogenase from ...
Escherichia coli K-12
Biochemistry
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1986
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Ray
L-Threonine dehydrogenase from ...
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Boylan
L-threonine dehydrogenase ...
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1981
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Aoyama
L-Threonine dehydrogenase of c ...
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J. Biol. Chem.
256
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1981
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Boylan
L-Threonine dehydrogenase of E ...
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McGilvray
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L-Threonine dehydrogenase (Art ...
Arthrobacter sp.
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285720
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The enzymatic formation of ami ...
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Hartshorne
Studies on liver threonine deh ...
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