BRENDA - Enzyme Database show
show all sequences of 1.1.1.103

Structure and function of the l-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis

Bowyer, A.; Mikolajek, H.; Stuart, J.W.; Wood, S.P.; Jamil, F.; Rashid, N.; Akhtar, M.; Cooper, J.B.; J. Struct. Biol. 168, 294-304 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant pET-tdh plasmid expressed in Escherichia coli BL21 (DE3)
Thermococcus kodakarensis
Crystallization (Commentary)
Crystallization
Organism
at room temperature using hanging-drop vapour diffusion method, at 2.4 A resolution. The enzyme is a homotetramer, each monomer consisting of 350 amino acids that form two domains, a catalytic domain and a NAD+-binding domain, which contains an alpha/beta Rossmann fold motif. An extended twelve-stranded beta-sheet is formed by the association of pairs of monomers in the tetramer
Thermococcus kodakarensis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
the active site catalytic zinc ion is absent from the TDH structure
Thermococcus kodakarensis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38016
-
4 * 38016, electrospray mass spectrometry and gel filtration
Thermococcus kodakarensis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermococcus kodakarensis
Q5JI69
-
-
Purification (Commentary)
Commentary
Organism
by sonication, heating of the cell lysate, anion exchange and hydrophobic interaction chromatography
Thermococcus kodakarensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-threonine + NAD+
-
699854
Thermococcus kodakarensis
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
homotetramer
4 * 38016, electrospray mass spectrometry and gel filtration
Thermococcus kodakarensis
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
binding site of the essential co-factor NAD+ is present in all subunits, it occupies the active site pocket and is bound predominantly by Van der Waal interactions and hydrogen bonds with the surrounding amino acid residues
Thermococcus kodakarensis
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant pET-tdh plasmid expressed in Escherichia coli BL21 (DE3)
Thermococcus kodakarensis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
binding site of the essential co-factor NAD+ is present in all subunits, it occupies the active site pocket and is bound predominantly by Van der Waal interactions and hydrogen bonds with the surrounding amino acid residues
Thermococcus kodakarensis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
at room temperature using hanging-drop vapour diffusion method, at 2.4 A resolution. The enzyme is a homotetramer, each monomer consisting of 350 amino acids that form two domains, a catalytic domain and a NAD+-binding domain, which contains an alpha/beta Rossmann fold motif. An extended twelve-stranded beta-sheet is formed by the association of pairs of monomers in the tetramer
Thermococcus kodakarensis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
the active site catalytic zinc ion is absent from the TDH structure
Thermococcus kodakarensis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38016
-
4 * 38016, electrospray mass spectrometry and gel filtration
Thermococcus kodakarensis
Purification (Commentary) (protein specific)
Commentary
Organism
by sonication, heating of the cell lysate, anion exchange and hydrophobic interaction chromatography
Thermococcus kodakarensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-threonine + NAD+
-
699854
Thermococcus kodakarensis
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homotetramer
4 * 38016, electrospray mass spectrometry and gel filtration
Thermococcus kodakarensis
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
-
-
1
1
5
-
-
4
1
-
-
1
-
4
-
-
1
-
-
1
-
-
1
-
-
-
-
2
-
-
-
1
-
-
-
-
-
1
1
1
5
-
-
-
-
4
1
-
-
1
-
-
-
1
-
1
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
5
5
737579
Lee
Effects of dietary levels of g ...
Gallus gallus
Asian-australas. J. Anim. Sci.
27
69-76
2014
-
-
-
-
-
-
-
-
1
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
738606
Nakano
Binding of NAD+ and L-threonin ...
Cupriavidus necator
J. Biol. Chem.
289
10445-10454
2014
-
-
1
1
3
-
-
5
-
-
-
1
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
1
-
-
-
1
-
-
-
-
-
1
1
1
3
-
-
-
-
5
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
3
3
738860
Ma
Identification and characteriz ...
Escherichia coli
J. Microbiol. Biotechnol.
24
748-755
2014
-
-
1
-
-
-
-
3
-
2
-
-
-
4
-
-
1
-
-
-
-
-
11
1
1
-
-
-
1
-
-
1
-
1
-
-
-
1
1
-
-
-
-
-
-
3
-
2
-
-
-
-
-
1
-
-
-
-
11
1
1
-
-
-
1
-
-
1
-
-
-
-
-
-
723777
Han
Regulation of L-threonine dehy ...
Mus musculus
Stem Cells
31
953-965
2013
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
722747
Yoneda
Crystal structure of binary an ...
Thermoplasma volcanium
J. Biol. Chem.
287
12966-12974
2012
1
-
1
1
-
-
2
2
-
-
3
1
-
5
-
-
-
1
-
-
-
-
1
1
1
-
1
-
1
-
1
1
-
-
-
1
-
1
1
1
-
-
-
2
-
2
-
-
3
1
-
-
-
-
-
-
-
-
1
1
1
-
1
-
1
-
1
-
-
1
1
-
-
-
721272
Ueatrongchit
Highly selective L-threonine 3 ...
Cupriavidus necator, Cupriavidus necator NBRC 102504
Anal. Biochem.
410
44-56
2011
2
-
1
-
-
-
14
2
-
13
2
2
-
8
-
-
1
-
-
-
2
-
6
1
1
1
1
2
1
1
1
1
-
-
-
2
-
1
1
-
-
-
-
14
-
2
-
13
2
2
-
-
-
1
-
-
2
-
6
1
1
1
1
2
1
1
1
-
-
2
2
-
-
-
698526
Bao
Biochemical characteristics an ...
Streptomyces sp. 139
J. Appl. Microbiol.
106
1140-1146
2009
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
1
2
-
1
-
1
-
1
-
1
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
2
-
1
-
1
-
1
-
1
-
-
-
-
-
-
-
698673
Bashir
Highly thermostable L-threonin ...
Thermococcus kodakarensis KOD1
J. Biochem.
146
95-102
2009
-
-
1
-
-
-
1
2
-
7
2
-
-
5
-
-
1
-
-
-
-
-
2
-
1
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
2
-
7
2
-
-
-
-
1
-
-
-
-
2
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
699854
Bowyer
Structure and function of the ...
Thermococcus kodakarensis
J. Struct. Biol.
168
294-304
2009
-
-
1
1
-
-
-
-
-
1
1
-
-
3
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
709827
Lee
Metabolic engineering of a red ...
Escherichia coli, Escherichia coli MDS42
Microb. Cell Fact.
8
02
2009
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
710562
Wang
Dependence of mouse embryonic ...
Mus musculus
Science
325
435-439
2009
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
687461
Higashi
Investigating a catalytic mech ...
Pyrococcus horikoshii
J. Biochem.
144
77-85
2008
-
-
1
-
7
-
-
8
-
1
1
1
-
2
-
-
1
1
-
-
-
-
2
1
1
-
-
7
1
1
-
1
-
-
-
-
-
1
1
-
7
-
-
-
-
8
-
1
1
1
-
-
-
1
-
-
-
-
2
1
1
-
-
7
1
1
-
-
-
-
-
-
-
-
695358
Bowyer
Crystallization and preliminar ...
Thermococcus kodakarensis
Acta Crystallogr. Sect. F
64
828-830
2008
-
-
1
1
-
-
-
-
-
-
1
-
-
5
-
-
1
-
-
-
-
1
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688343
Ishikawa
The first crystal structure of ...
Pyrococcus horikoshii
J. Mol. Biol.
366
857-867
2007
-
-
1
1
2
-
-
6
-
1
1
1
-
3
-
-
-
-
-
-
-
-
1
2
1
-
-
6
1
-
-
2
-
-
-
-
-
1
2
1
2
-
-
-
-
6
-
1
1
1
-
-
-
-
-
-
-
-
1
2
1
-
-
6
1
-
-
-
-
-
-
-
-
-
668567
Machielsen
Production and characterizatio ...
Pyrococcus furiosus
FEBS J.
273
2722-2729
2006
-
-
1
-
-
-
1
2
-
2
3
1
-
4
-
-
1
1
-
-
-
-
6
1
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
2
-
2
3
1
-
-
-
1
-
-
-
-
6
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
667071
Higashi
Crystallization and preliminar ...
Pyrococcus horikoshii
Acta crystallogr. Sect. F
61
432-434
2005
-
-
1
1
-
-
-
-
-
1
1
-
-
4
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
668111
Le Floch
Catabolism through the threoni ...
Sus scrofa
Br. J. Nutr.
93
447-456
2005
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
6
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
6
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668536
Shimizu
L-Threonine dehydrogenase from ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Extremophiles
9
317-324
2005
-
-
1
-
-
-
1
-
-
3
3
2
-
45
-
-
1
1
-
-
1
-
10
1
1
-
4
-
1
1
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
3
3
2
-
-
-
1
-
-
1
-
10
1
1
-
4
-
1
1
-
-
-
-
-
-
-
-
669546
Higashi
Kinetic study of thermostable ...
Pyrococcus horikoshii
J. Biosci. Bioeng.
99
175-180
2005
-
-
1
-
-
-
1
3
-
4
2
1
-
3
-
-
1
-
-
-
-
-
1
1
1
1
1
4
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
3
-
4
2
1
-
-
-
1
-
-
-
-
1
1
1
1
1
4
1
-
-
-
-
-
-
-
-
-
654175
Akagi
Threonine metabolism in Japane ...
Coturnix japonica, Rattus norvegicus
Amino Acids
26
235-242
2004
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655857
Kazuoka
Novel psychrophilic and thermo ...
Cytophaga sp., Cytophaga sp. KUC-1
J. Bacteriol.
185
4483-4489
2003
-
-
1
-
-
-
9
5
-
-
2
-
-
8
-
-
1
1
-
-
5
1
12
1
1
1
3
-
1
2
-
3
4
-
-
-
-
1
3
-
-
-
-
9
4
5
-
-
2
-
-
-
-
1
-
-
5
1
12
1
1
1
3
-
1
2
-
-
-
-
-
-
-
-
655125
Edgar
Molecular cloning and tissue d ...
Mus musculus, Sus scrofa
BMC Biochem.
3
19
2002
-
-
-
-
-
-
-
-
-
-
3
-
-
8
-
1
-
-
-
8
-
-
-
2
-
-
-
-
-
-
-
2
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
8
-
-
-
2
-
-
-
-
-
-
-
2
-
-
-
-
-
-
655131
Edgar
The human L-threonine 3-dehydr ...
Homo sapiens
BMC Genet.
3
18
2002
-
-
-
-
1
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285701
Yuan
Characterization of hepatic L- ...
Gallus gallus
Comp. Biochem. Physiol. B
130
65-73
2001
-
-
-
-
-
-
-
2
1
-
2
1
-
3
-
-
1
-
-
2
1
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
2
1
-
2
1
-
-
-
1
-
2
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285702
Johnson
Investigation of a catalytic z ...
Escherichia coli K-12
Arch. Biochem. Biophys.
358
211-221
1998
-
-
-
-
2
-
2
1
-
4
1
1
-
2
-
-
1
-
-
-
7
-
6
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
1
-
2
-
-
2
-
1
-
4
1
1
-
-
-
1
-
-
7
-
6
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
285703
Marcus
Identification of a second act ...
Escherichia coli K-12
Arch. Biochem. Biophys.
316
413-420
1995
-
-
-
-
-
-
1
2
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285704
Chen
Functional analysis of E. coli ...
Escherichia coli K-12
Biochim. Biophys. Acta
1253
208-214
1995
-
-
-
-
1
-
-
-
-
1
-
1
-
7
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
729112
Wagner
Purification and characterizat ...
Clostridium sticklandii, Clostridium sticklandii DSM 519
Arch. Microbiol.
163
286-290
1995
-
-
-
-
-
-
4
2
-
-
2
2
-
5
-
-
1
-
-
-
1
-
8
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
-
-
-
4
-
2
-
-
2
2
-
-
-
1
-
-
1
-
8
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
285705
Kao
Purification and structural ch ...
Sus scrofa
Protein Expr. Purif.
5
423-431
1994
-
-
-
-
-
-
-
-
1
-
2
1
-
2
-
-
1
-
-
2
1
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
2
1
-
-
-
1
-
2
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285706
Marcus
Threonine formation via the co ...
Escherichia coli K-12
J. Bacteriol.
175
6505-6511
1993
-
-
-
-
-
-
1
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285707
Pagani
-
Mitochondrial L-threonine dehy ...
Rattus norvegicus
Biochem. Soc. Trans.
20
379
1992
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
1
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285708
Pagani
-
Rat liver L-threonine dehydrog ...
Bos taurus, Rattus norvegicus
Biochem. Soc. Trans.
20
24
1991
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
2
3
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
3
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
285709
Epperly
L-Threonine dehydrogenase from ...
Escherichia coli K-12
J. Biol. Chem.
266
6086-6092
1991
-
-
-
-
-
-
4
-
-
1
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285710
Craig
The sulfhydryl content of L-th ...
Escherichia coli K-12
Biochim. Biophys. Acta
1037
30-38
1990
-
-
-
-
-
-
5
-
-
1
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
5
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285711
Aronson
The primary structure of Esche ...
Escherichia coli K-12
J. Biol. Chem.
264
5226-5232
1989
-
-
1
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285712
Craig
Cd2+ activation of L-threonine ...
Escherichia coli K-12
Biochim. Biophys. Acta
957
222-229
1988
-
-
-
-
-
-
-
6
-
1
-
1
-
2
-
-
-
-
-
-
3
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
6
-
1
-
1
-
-
-
-
-
-
3
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285713
Tressel
Interaction between L-threonin ...
Sus scrofa
J. Biol. Chem.
261
16428-16437
1986
-
-
-
-
-
-
3
3
-
-
-
1
-
1
-
-
-
1
-
1
-
-
2
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
3
-
3
-
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
285714
Craig
L-Threonine dehydrogenase from ...
Escherichia coli K-12
Biochemistry
25
1870-1876
1986
-
-
-
-
-
-
5
4
-
2
-
1
-
3
-
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
5
-
4
-
2
-
1
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285715
Ray
L-Threonine dehydrogenase from ...
Capra hircus
J. Biol. Chem.
260
5913-5918
1985
-
-
-
-
-
-
1
2
-
-
3
1
-
2
-
-
1
-
-
2
1
-
1
2
-
-
-
-
1
1
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
2
-
-
3
1
-
-
-
1
-
2
1
-
1
2
-
-
-
-
1
1
-
-
-
-
-
-
-
-
285716
Boylan
L-threonine dehydrogenase ...
Escherichia coli K-12
J. Biol. Chem.
256
1809-1815
1981
-
-
-
-
-
-
5
2
-
1
1
1
-
4
-
-
1
-
-
-
1
-
9
-
-
-
-
1
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
5
-
2
-
1
1
1
-
-
-
1
-
-
1
-
9
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
285717
Aoyama
L-Threonine dehydrogenase of c ...
Gallus gallus
J. Biol. Chem.
256
12367-12373
1981
-
-
-
-
-
-
7
2
1
-
2
1
-
3
-
-
1
-
-
2
1
1
1
1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
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
-
-
1
1
-
2
-
-
1
-
-
-
1
1
7
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
1
1
-
-
-
1
-
-
1
1
7
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
285719
McGilvray
-
L-Threonine dehydrogenase (Art ...
Arthrobacter sp.
Methods Enzymol.
17B
580-584
1971
-
-
-
-
-
1
4
2
-
3
-
1
-
1
-
-
1
-
-
-
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
1
-
4
-
2
-
3
-
1
-
-
-
1
-
-
1
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
285720
Green
The enzymatic formation of ami ...
Gallus gallus, Oryctolagus cuniculus, Rattus norvegicus, Staphylococcus aureus, Sus scrofa
biochem. J.
92
537-548
1964
-
-
-
-
-
-
-
2
-
-
-
5
-
5
-
-
1
-
-
7
1
-
5
-
-
-
1
-
1
-
-
5
-
-
-
-
-
-
5
-
-
-
-
-
-
2
-
-
-
5
-
-
-
1
-
7
1
-
5
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
285721
Hartshorne
Studies on liver threonine deh ...
Rana catesbeiana
Arch. Biochem. Biophys.
105
173-178
1964
-
-
-
-
-
-
4
2
-
-
-
1
-
1
-
-
1
-
-
1
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
4
-
2
-
-
-
1
-
-
-
1
-
1
1
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-