BRENDA - Enzyme Database show
show all sequences of 1.1.1.3

Structural insight into activation of homoserine dehydrogenase from the archaeon

Tomonaga, Y.; Kaneko, R.; Goto, M.; Ohshima, T.; Yoshimune, K.; Biochem. Biophys. Rep. 3, 14-17 (2015)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
dithiothreitol
the enzyme is 2.5fold activated by the addition of 0.8 mM dithiothreitol. The activation is caused by cleavage of the disulfide bond formed between two cysteine residues in the C-terminal regions of the two subunits
Sulfurisphaera tokodaii
Cloned(Commentary)
Commentary
Organism
gene hom, recombinant overexpression in Escherichia coli strain BL21(DE3)
Sulfurisphaera tokodaii
Crystallization (Commentary)
Crystallization
Organism
purified recombinant enzyme in oxidized and in reduced form, hanging drop vapor diffusion method, for the oxidized form: mixing of 0.0015 ml of 5.9 mg/ml protein solution with 0.0015 ml of reservoir solution, pH 4.1, containing 9.5% w/v PEG 3350, 19% w/v PEG 400, 0.19 M magnesium chloride, and 2.5% DMSO, for the reduced form: soaking of the oxidized enzyme crystals in a solution consisting of 0.003 ml of reservoir solution and 0.001 ml of 200 mM DTT for 60 min prior to the first diffraction data collection, 12C, X-ray diffraction structure determmination and analysis at 1.60-1.83 A resolution, molecular replacement and modelling
Sulfurisphaera tokodaii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.21
-
L-homoserine
pH 8.0, 30C, oxidized enzyme
Sulfurisphaera tokodaii
0.31
-
NAD+
pH 8.0, 30C, oxidized enzyme
Sulfurisphaera tokodaii
0.33
-
NAD+
pH 8.0, 30C, reduced enzyme
Sulfurisphaera tokodaii
0.54
-
L-homoserine
pH 8.0, 30C, reduced enzyme
Sulfurisphaera tokodaii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-homoserine + NAD(P)+
Sulfurisphaera tokodaii
-
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
r
L-homoserine + NAD(P)+
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sulfurisphaera tokodaii
F9VNG5
-
-
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
F9VNG5
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment at 70C for 3 h, anion exchange chromatography, dialysis, and ultrafiltration
Sulfurisphaera tokodaii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-homoserine + NAD(P)+
-
739972
Sulfurisphaera tokodaii
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
-
r
L-homoserine + NAD(P)+
-
739972
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
-
r
L-homoserine + NAD+
-
739972
Sulfurisphaera tokodaii
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
-
739972
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
Subunits
Subunits
Commentary
Organism
homodimer
dimeric enzyme structure, overview
Sulfurisphaera tokodaii
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Sulfurisphaera tokodaii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Sulfurisphaera tokodaii
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Sulfurisphaera tokodaii
NADH
-
Sulfurisphaera tokodaii
NADP+
-
Sulfurisphaera tokodaii
NADPH
-
Sulfurisphaera tokodaii
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
dithiothreitol
the enzyme is 2.5fold activated by the addition of 0.8 mM dithiothreitol. The activation is caused by cleavage of the disulfide bond formed between two cysteine residues in the C-terminal regions of the two subunits
Sulfurisphaera tokodaii
Cloned(Commentary) (protein specific)
Commentary
Organism
gene hom, recombinant overexpression in Escherichia coli strain BL21(DE3)
Sulfurisphaera tokodaii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Sulfurisphaera tokodaii
NADH
-
Sulfurisphaera tokodaii
NADP+
-
Sulfurisphaera tokodaii
NADPH
-
Sulfurisphaera tokodaii
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant enzyme in oxidized and in reduced form, hanging drop vapor diffusion method, for the oxidized form: mixing of 0.0015 ml of 5.9 mg/ml protein solution with 0.0015 ml of reservoir solution, pH 4.1, containing 9.5% w/v PEG 3350, 19% w/v PEG 400, 0.19 M magnesium chloride, and 2.5% DMSO, for the reduced form: soaking of the oxidized enzyme crystals in a solution consisting of 0.003 ml of reservoir solution and 0.001 ml of 200 mM DTT for 60 min prior to the first diffraction data collection, 12C, X-ray diffraction structure determmination and analysis at 1.60-1.83 A resolution, molecular replacement and modelling
Sulfurisphaera tokodaii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.21
-
L-homoserine
pH 8.0, 30C, oxidized enzyme
Sulfurisphaera tokodaii
0.31
-
NAD+
pH 8.0, 30C, oxidized enzyme
Sulfurisphaera tokodaii
0.33
-
NAD+
pH 8.0, 30C, reduced enzyme
Sulfurisphaera tokodaii
0.54
-
L-homoserine
pH 8.0, 30C, reduced enzyme
Sulfurisphaera tokodaii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-homoserine + NAD(P)+
Sulfurisphaera tokodaii
-
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
r
L-homoserine + NAD(P)+
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment at 70C for 3 h, anion exchange chromatography, dialysis, and ultrafiltration
Sulfurisphaera tokodaii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-homoserine + NAD(P)+
-
739972
Sulfurisphaera tokodaii
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
-
r
L-homoserine + NAD(P)+
-
739972
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
-
r
L-homoserine + NAD+
-
739972
Sulfurisphaera tokodaii
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
-
739972
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
dimeric enzyme structure, overview
Sulfurisphaera tokodaii
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Sulfurisphaera tokodaii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Sulfurisphaera tokodaii
General Information
General Information
Commentary
Organism
physiological function
homoserine dehydrogenase catalyzes an NAD(P)-dependent reversible reaction between L-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway
Sulfurisphaera tokodaii
General Information (protein specific)
General Information
Commentary
Organism
physiological function
homoserine dehydrogenase catalyzes an NAD(P)-dependent reversible reaction between L-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway
Sulfurisphaera tokodaii
Other publictions for EC 1.1.1.3
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)
740860
Tsai
Candida albicans Hom6 is a hom ...
Candida albicans, Candida albicans SC5314 / ATCC MYA-2876
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2
1
-
1
-
-
-
2
-
-
2
-
5
-
-
-
-
-
-
-
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2
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1
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1
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2
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2
1
2
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1
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2
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2
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-
-
2
-
1
-
-
-
1
-
-
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2
2
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-
738802
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Characterization of aspartate ...
Corynebacterium glutamicum, Corynebacterium glutamicum IWJ001
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43
873-885
2016
-
-
1
-
2
-
1
-
-
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2
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4
-
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2
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2
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1
2
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2
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1
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2
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1
1
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739779
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Rational design of allosteric ...
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4
126-131
2015
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1
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3
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2
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1
1
-
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-
739791
Navratna
Structural basis for the catal ...
Staphylococcus aureus, Staphylococcus aureus COL
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71
1216-1225
2015
-
-
1
1
3
-
2
1
-
-
-
2
-
4
-
-
1
1
-
-
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2
2
1
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1
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2
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1
2
1
3
-
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2
-
1
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2
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-
1
-
-
-
-
2
2
1
-
-
-
1
-
-
-
-
3
3
-
-
-
739972
Tomonaga
Structural insight into activa ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
Biochem. Biophys. Rep.
3
14-17
2015
1
-
1
1
-
-
-
4
-
-
-
2
-
2
-
-
1
-
-
-
-
-
4
1
1
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1
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4
-
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-
1
-
1
4
1
-
-
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4
-
-
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2
-
-
-
1
-
-
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-
4
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
741408
Hayashi
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Pyrococcus horikoshii, Pyrococcus horikoshii ATCC 700860
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5
11674
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-
-
1
1
2
-
1
7
-
-
2
2
-
2
-
-
1
-
-
-
-
-
4
1
1
-
2
5
1
-
1
5
1
-
-
-
-
1
5
1
2
-
-
1
1
7
-
-
2
2
-
-
-
1
-
-
-
-
4
1
1
-
2
5
1
-
1
-
-
1
1
-
5
5
740548
Zhan
Exploring the molecular basis ...
Mycobacterium leprae, Mycobacterium leprae TN
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15
1826-1841
2014
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-
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7
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2
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5
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2
1
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2
5
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2
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1
7
5
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2
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2
1
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-
1
1
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741465
Shen
Heterologous expression and ch ...
Corynebacterium pekinense, Corynebacterium pekinense AS1.299
Wei Sheng Wu Xue Bao
54
1178-1184
2014
-
-
1
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5
-
-
-
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1
2
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2
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1
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1
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1
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5
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1
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2
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1
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1
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-
-
739804
Navratna
Crystallization and preliminar ...
Staphylococcus aureus, Staphylococcus aureus COL
Acta Crystallogr. Sect. F
69
1216-1219
2013
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1
1
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1
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2
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4
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1
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2
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1
2
1
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1
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2
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1
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2
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2
2
-
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710978
Brautaset
Bacillus methanolicus pyruvate ...
Bacillus methanolicus, Bacillus methanolicus MGA3
Appl. Microbiol. Biotechnol.
87
951-964
2010
-
1
-
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1
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-
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-
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6
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1
1
1
2
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712490
Schroeder
Threonine-insensitive homoseri ...
Glycine max
J. Biol. Chem.
285
827-834
2010
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1
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2
23
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3
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5
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1
1
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1
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15
1
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12
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2
1
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3
2
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2
1
24
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3
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3
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1
-
15
1
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12
-
-
-
-
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-
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24
24
688167
Yilmaz
Targeted disruption of homoser ...
Streptomyces clavuligerus, Streptomyces clavuligerus NRRL 3585
J. Ind. Microbiol. Biotechnol.
35
1-7
2008
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1
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1
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2
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5
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1
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689647
Varisi
Lysine biosynthesis and nitrog ...
Chenopodium quinoa
Plant Physiol. Biochem.
46
11-18
2008
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2
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3
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1
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1
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1
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688822
Park
Characteristics of methionine ...
Corynebacterium glutamicum
Metab. Eng.
9
327-336
2007
-
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1
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1
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1
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3
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1
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1
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670165
Cahyanto
Regulation of aspartokinase, a ...
Lactobacillus plantarum
Microbiology
152
105-112
2006
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1
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2
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3
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1
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2
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662432
Curien
Identification of six novel al ...
Arabidopsis thaliana
J. Biol. Chem.
280
41178-41183
2005
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1
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1
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4
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1
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1
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1
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1
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Homoserine dehydrogenase from ...
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Comparison of homoserine dehyd ...
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Reaction of Tris with aldehyde ...
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Threonine-sensitive aspartate ...
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Properties of homoserine dehyd ...
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