BRENDA - Enzyme Database show
show all sequences of 1.1.1.103

L-Threonine dehydrogenase from Escherichia coli K-12: thiol-dependent activation by Mn2+

Craig, P.A.; Dekker, E.E.; Biochemistry 25, 1870-1876 (1986)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Ag+
0.064 mM, activity is completely blocked
Escherichia coli K-12
Be2+
3.2 mM, 20-50% inhibition
Escherichia coli K-12
Cu2+
3.2 mM, 20-50% inhibition
Escherichia coli K-12
Hg2+
0.064 mM, activity is completely blocked
Escherichia coli K-12
Ni2+
3.2 mM, 20-50% inhibition
Escherichia coli K-12
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.11
-
NAD+
demetallized enzyme
Escherichia coli K-12
0.6
-
NAD+
enzyme saturated with 0.25 mM Mn2+
Escherichia coli K-12
1.1
-
L-threonine
demetallized enzyme
Escherichia coli K-12
221
-
L-threonine
enzyme saturated with 0.25 mM Mn2+
Escherichia coli K-12
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Cd2+
0.064 or 3.2 mM, 6fold increase of L-threonine dehydrogenase activity
Escherichia coli K-12
Mn2+
0.064 or 3.2 mM, 4fold increase of L-threonine dehydrogenase activity, activation is dependent on the presence of a reduced thiol in all enzyme stock solutions and assay buffers, binding of 0.86 mol of Mn2+ per mol of enzyme subunit
Escherichia coli K-12
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-threonine + NAD+
Escherichia coli K-12
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
Escherichia coli K-12
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli K-12
-
-
-
Purification (Commentary)
Commentary
Organism
-
Escherichia coli K-12
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
8
-
fully demetalized enzyme
Escherichia coli K-12
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-threonine + NAD+
-
285714
Escherichia coli K-12
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
285714
Escherichia coli K-12
-
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli K-12
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli K-12
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ag+
0.064 mM, activity is completely blocked
Escherichia coli K-12
Be2+
3.2 mM, 20-50% inhibition
Escherichia coli K-12
Cu2+
3.2 mM, 20-50% inhibition
Escherichia coli K-12
Hg2+
0.064 mM, activity is completely blocked
Escherichia coli K-12
Ni2+
3.2 mM, 20-50% inhibition
Escherichia coli K-12
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.11
-
NAD+
demetallized enzyme
Escherichia coli K-12
0.6
-
NAD+
enzyme saturated with 0.25 mM Mn2+
Escherichia coli K-12
1.1
-
L-threonine
demetallized enzyme
Escherichia coli K-12
221
-
L-threonine
enzyme saturated with 0.25 mM Mn2+
Escherichia coli K-12
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Cd2+
0.064 or 3.2 mM, 6fold increase of L-threonine dehydrogenase activity
Escherichia coli K-12
Mn2+
0.064 or 3.2 mM, 4fold increase of L-threonine dehydrogenase activity, activation is dependent on the presence of a reduced thiol in all enzyme stock solutions and assay buffers, binding of 0.86 mol of Mn2+ per mol of enzyme subunit
Escherichia coli K-12
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-threonine + NAD+
Escherichia coli K-12
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
Escherichia coli K-12
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli K-12
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
8
-
fully demetalized enzyme
Escherichia coli K-12
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-threonine + NAD+
-
285714
Escherichia coli K-12
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
285714
Escherichia coli K-12
-
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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737579
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Effects of dietary levels of g ...
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738606
Nakano
Binding of NAD+ and L-threonin ...
Cupriavidus necator
J. Biol. Chem.
289
10445-10454
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738860
Ma
Identification and characteriz ...
Escherichia coli
J. Microbiol. Biotechnol.
24
748-755
2014
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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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722747
Yoneda
Crystal structure of binary an ...
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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14
2
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13
2
2
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8
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1
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1
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14
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1
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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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698673
Bashir
Highly thermostable L-threonin ...
Thermococcus kodakarensis KOD1
J. Biochem.
146
95-102
2009
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1
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2
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7
2
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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
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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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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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1
1
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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
2
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6
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1
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1
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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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1
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667071
Higashi
Crystallization and preliminar ...
Pyrococcus horikoshii
Acta crystallogr. Sect. F
61
432-434
2005
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1
1
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1
1
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4
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1
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1
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668111
Le Floch
Catabolism through the threoni ...
Sus scrofa
Br. J. Nutr.
93
447-456
2005
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1
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1
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668536
Shimizu
L-Threonine dehydrogenase from ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Extremophiles
9
317-324
2005
-
-
1
-
-
-
1
-
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3
3
2
-
45
-
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1
1
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1
-
10
1
1
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4
-
1
1
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1
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1
1
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1
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3
3
2
-
-
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1
-
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1
-
10
1
1
-
4
-
1
1
-
-
-
-
-
-
-
-
669546
Higashi
Kinetic study of thermostable ...
Pyrococcus horikoshii
J. Biosci. Bioeng.
99
175-180
2005
-
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1
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1
3
-
4
2
1
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3
-
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1
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1
1
1
1
1
4
1
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1
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1
1
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1
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3
-
4
2
1
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1
-
-
-
-
1
1
1
1
1
4
1
-
-
-
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-
-
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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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2
2
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2
2
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655857
Kazuoka
Novel psychrophilic and thermo ...
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2003
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655125
Edgar
Molecular cloning and tissue d ...
Mus musculus, Sus scrofa
BMC Biochem.
3
19
2002
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655131
Edgar
The human L-threonine 3-dehydr ...
Homo sapiens
BMC Genet.
3
18
2002
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285701
Yuan
Characterization of hepatic L- ...
Gallus gallus
Comp. Biochem. Physiol. B
130
65-73
2001
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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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285703
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Identification of a second act ...
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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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285705
Kao
Purification and structural ch ...
Sus scrofa
Protein Expr. Purif.
5
423-431
1994
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285706
Marcus
Threonine formation via the co ...
Escherichia coli K-12
J. Bacteriol.
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1993
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Pagani
-
Mitochondrial L-threonine dehy ...
Rattus norvegicus
Biochem. Soc. Trans.
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379
1992
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285708
Pagani
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Rat liver L-threonine dehydrog ...
Bos taurus, Rattus norvegicus
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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.
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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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4
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285715
Ray
L-Threonine dehydrogenase from ...
Capra hircus
J. Biol. Chem.
260
5913-5918
1985
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285716
Boylan
L-threonine dehydrogenase ...
Escherichia coli K-12
J. Biol. Chem.
256
1809-1815
1981
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285717
Aoyama
L-Threonine dehydrogenase of c ...
Gallus gallus
J. Biol. Chem.
256
12367-12373
1981
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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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285719
McGilvray
-
L-Threonine dehydrogenase (Art ...
Arthrobacter sp.
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580-584
1971
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285720
Green
The enzymatic formation of ami ...
Gallus gallus, Oryctolagus cuniculus, Rattus norvegicus, Staphylococcus aureus, Sus scrofa
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537-548
1964
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5
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Hartshorne
Studies on liver threonine deh ...
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Arch. Biochem. Biophys.
105
173-178
1964
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