BRENDA - Enzyme Database show
show all sequences of 1.1.1.3

Threonine-insensitive homoserine dehydrogenase from soybean: genomic organization, kinetic mechanism, and in vivo activity

Schroeder, A.C.; Zhu, C.; Yanamadala, S.R.; Cahoon, R.E.; Arkus, K.A.; Wachsstock, L.; Bleeke, J.; Krishnan, H.B.; Jez, J.M.; J. Biol. Chem. 285, 827-834 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
Glycine max
Inhibitors
Inhibitors
Commentary
Organism
Structure
L-threonine
-
Glycine max
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
Glycine max
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.028
-
NADPH
pH 8.0, 25C
Glycine max
0.034
-
NADP+
pH 8.0, 25C
Glycine max
0.039
-
NADPH
pH 8.0, 25C; pH 8.0, 25C
Glycine max
0.098
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
0.158
-
NADH
pH 8.0, 25C
Glycine max
0.19
-
NADH
pH 8.0, 25C
Glycine max
0.213
-
NADH
pH 8.0, 25C
Glycine max
0.235
-
NADP+
pH 8.0, 25C
Glycine max
0.245
-
NADP+
pH 8.0, 25C
Glycine max
0.275
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.569
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
0.69
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.845
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.08
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.19
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.25
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
2.19
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
2.7
-
NAD+
pH 8.0, 25C
Glycine max
9.57
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
13.4
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
17.4
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
24.1
-
NAD+
pH 8.0, 25C
Glycine max
24.9
-
NAD+
pH 8.0, 25C
Glycine max
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
2 * 40600, calculated, 2 * 40000, SDS-PAGE
Glycine max
40600
-
2 * 40600, calculated, 2 * 40000, SDS-PAGE
Glycine max
70000
-
gel filtration
Glycine max
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Glycine max
O63067
bifunctional aspartokinase-homoserine dehydrogenase AK-HSD-2
-
Glycine max
O65027
bifunctional aspartokinase-homoserine dehydrogenase AK-HSD-1
-
Glycine max
Q3S3F6
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme; recombinant enzyme; recombinant enzyme
Glycine max
Reaction
Reaction
Commentary
Organism
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
ordered bi bi kinetic mechanism in which nicotinamide cofactor binds first and leaves last in the reaction sequence
Glycine max
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
13
-
pH 8.0, 25C
Glycine max
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-aspartate 4-semialdehyde + NADH
-
712490
Glycine max
L-homoserine + NAD+
-
-
-
r
L-aspartate 4-semialdehyde + NADPH
-
712490
Glycine max
L-homoserine + NADP+
-
-
-
r
L-homoserine + NAD+
-
712490
Glycine max
L-aspartate 4-semialdehyde + NADH
-
-
-
r
L-homoserine + NADP+
-
712490
Glycine max
L-aspartate 4-semialdehyde + NADPH
-
-
-
r
additional information
enzyme does not show aspartate kinase activity
712490
Glycine max
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
2 * 40600, calculated, 2 * 40000, SDS-PAGE
Glycine max
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.042
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.052
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.07
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.43
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
2.8
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
7
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
9.68
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
10.15
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
11.58
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
12.98
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
19.3
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
22.58
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
GmHSD displays a 1.6fold preference for NADPH over NADH as the cofactor in the oxidation reaction. In the reduction reaction NADP+ is favored nearly 4fold as the cofactor
Glycine max
NADPH
GmHSD displays a 1.6fold preference for NADPH over NADH as the cofactor in the oxidation reaction. In the reduction reaction NADP+ is favored nearly 4fold as the cofactor
Glycine max
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
160
240
L-threonine
pH 8.0, 25C
Glycine max
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Glycine max
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
GmHSD displays a 1.6fold preference for NADPH over NADH as the cofactor in the oxidation reaction. In the reduction reaction NADP+ is favored nearly 4fold as the cofactor
Glycine max
NADPH
GmHSD displays a 1.6fold preference for NADPH over NADH as the cofactor in the oxidation reaction. In the reduction reaction NADP+ is favored nearly 4fold as the cofactor
Glycine max
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
L-threonine
-
Glycine max
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
Glycine max
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
160
240
L-threonine
pH 8.0, 25C
Glycine max
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.028
-
NADPH
pH 8.0, 25C
Glycine max
0.034
-
NADP+
pH 8.0, 25C
Glycine max
0.039
-
NADPH
pH 8.0, 25C
Glycine max
0.098
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
0.158
-
NADH
pH 8.0, 25C
Glycine max
0.19
-
NADH
pH 8.0, 25C
Glycine max
0.213
-
NADH
pH 8.0, 25C
Glycine max
0.235
-
NADP+
pH 8.0, 25C
Glycine max
0.245
-
NADP+
pH 8.0, 25C
Glycine max
0.275
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.569
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
0.69
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.845
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.08
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.19
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.25
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
2.19
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
2.7
-
NAD+
pH 8.0, 25C
Glycine max
9.57
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
13.4
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
17.4
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
24.1
-
NAD+
pH 8.0, 25C
Glycine max
24.9
-
NAD+
pH 8.0, 25C
Glycine max
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
2 * 40600, calculated, 2 * 40000, SDS-PAGE
Glycine max
40600
-
2 * 40600, calculated, 2 * 40000, SDS-PAGE
Glycine max
70000
-
gel filtration
Glycine max
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme
Glycine max
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
13
-
pH 8.0, 25C
Glycine max
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-aspartate 4-semialdehyde + NADH
-
712490
Glycine max
L-homoserine + NAD+
-
-
-
r
L-aspartate 4-semialdehyde + NADPH
-
712490
Glycine max
L-homoserine + NADP+
-
-
-
r
L-homoserine + NAD+
-
712490
Glycine max
L-aspartate 4-semialdehyde + NADH
-
-
-
r
L-homoserine + NADP+
-
712490
Glycine max
L-aspartate 4-semialdehyde + NADPH
-
-
-
r
additional information
enzyme does not show aspartate kinase activity
712490
Glycine max
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 40600, calculated, 2 * 40000, SDS-PAGE
Glycine max
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.042
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.052
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.07
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.43
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
2.8
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
7
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
9.68
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
10.15
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
11.58
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
12.98
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
19.3
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
22.58
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.039
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.082
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
0.095
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.18
-
NADP+
pH 8.0, 25C
Glycine max
0.256
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.268
-
NADP+
pH 8.0, 25C
Glycine max
0.281
-
NAD+
pH 8.0, 25C
Glycine max
0.421
-
NAD+
pH 8.0, 25C
Glycine max
0.53
-
NAD+
pH 8.0, 25C
Glycine max
0.731
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
0.757
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
2.07
-
NADP+
pH 8.0, 25C
Glycine max
5.29
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
10.39
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
16.22
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
17.02
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
26.73
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
28.54
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
61.29
-
NADH
pH 8.0, 25C
Glycine max
90.61
-
NADH
pH 8.0, 25C
Glycine max
101.4
-
NADPH
pH 8.0, 25C
Glycine max
118.9
-
NADH
pH 8.0, 25C
Glycine max
296.2
-
NADPH
pH 8.0, 25C
Glycine max
331.2
-
NADPH
pH 8.0, 25C
Glycine max
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.039
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.082
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
0.095
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.18
-
NADP+
pH 8.0, 25C
Glycine max
0.256
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
0.268
-
NADP+
pH 8.0, 25C
Glycine max
0.281
-
NAD+
pH 8.0, 25C
Glycine max
0.421
-
NAD+
pH 8.0, 25C
Glycine max
0.53
-
NAD+
pH 8.0, 25C
Glycine max
0.731
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
0.757
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
2.07
-
NADP+
pH 8.0, 25C
Glycine max
5.29
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
10.39
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
16.22
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
17.02
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
26.73
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
28.54
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
61.29
-
NADH
pH 8.0, 25C
Glycine max
90.61
-
NADH
pH 8.0, 25C
Glycine max
101.4
-
NADPH
pH 8.0, 25C
Glycine max
118.9
-
NADH
pH 8.0, 25C
Glycine max
296.2
-
NADPH
pH 8.0, 25C
Glycine max
331.2
-
NADPH
pH 8.0, 25C
Glycine max
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)
710978
Brautaset
Bacillus methanolicus pyruvate ...
Bacillus methanolicus, Bacillus methanolicus MGA3
Appl. Microbiol. Biotechnol.
87
951-964
2010
-
1
-
-
1
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
2
-
-
712490
Schroeder
Threonine-insensitive homoseri ...
Glycine max
J. Biol. Chem.
285
827-834
2010
-
-
1
-
-
-
2
23
-
-
3
-
-
5
-
-
1
1
-
-
1
-
15
1
-
-
-
12
-
-
-
2
1
-
-
-
-
3
2
-
-
-
-
2
1
24
-
-
3
-
-
-
-
3
-
-
1
-
15
1
-
-
-
12
-
-
-
-
-
-
-
-
24
24
688167
Yilmaz
Targeted disruption of homoser ...
Streptomyces clavuligerus, Streptomyces clavuligerus NRRL 3585
J. Ind. Microbiol. Biotechnol.
35
1-7
2008
-
-
1
-
1
-
-
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
689647
Varisi
Lysine biosynthesis and nitrog ...
Chenopodium quinoa
Plant Physiol. Biochem.
46
11-18
2008
-
-
-
-
-
-
2
-
-
-
-
-
-
3
-
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688822
Park
Characteristics of methionine ...
Corynebacterium glutamicum
Metab. Eng.
9
327-336
2007
-
-
1
-
1
-
1
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-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
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1
-
-
1
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
670165
Cahyanto
Regulation of aspartokinase, a ...
Lactobacillus plantarum
Microbiology
152
105-112
2006
-
-
1
-
-
-
2
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
662432
Curien
Identification of six novel al ...
Arabidopsis thaliana
J. Biol. Chem.
280
41178-41183
2005
-
-
1
-
-
-
1
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
654955
Ejim
New phenolic inhibitors of yea ...
Saccharomyces cerevisiae
Bioorg. Med. Chem.
12
3825-3830
2004
-
1
-
1
-
-
13
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
2
1
-
-
-
13
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642341
Paris
Mechanism of control of Arabid ...
Arabidopsis thaliana
J. Biol. Chem.
278
5361-5366
2003
-
-
-
-
2
-
1
-
-
1
2
-
-
2
-
-
-
1
-
-
-
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
1
2
-
-
-
-
-
-
-
-
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
657018
Rognes
Transcriptional and biochemica ...
Arabidopsis thaliana, Saccharomyces cerevisiae
Plant Mol. Biol.
51
281-294
2003
-
-
1
-
2
-
1
-
-
1
-
2
-
6
-
-
-
1
-
4
-
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
3
-
2
-
-
1
-
-
-
1
-
2
-
-
-
-
-
4
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642340
Paris
Overproduction, purification, ...
Arabidopsis thaliana
Protein Expr. Purif.
24
105-110
2002
-
-
-
-
-
-
1
5
-
1
2
-
-
3
-
-
-
1
-
-
2
1
1
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
5
-
1
2
-
-
-
-
-
-
-
2
1
1
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
654640
James
Production and characterizatio ...
Escherichia coli
Biochemistry
41
3720-3725
2002
-
-
1
-
1
-
-
4
-
-
-
1
-
2
-
-
1
1
-
-
-
-
2
-
-
-
-
4
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
4
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
246401
Jacques
Homoserine dehydrogenase from ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1544
42-54
2001
-
-
-
-
-
-
4
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246402
Jacques
Characterization of yeast homo ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1544
28-41
2001
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246396
DeLaBarre
Crystal structures of homoseri ...
Saccharomyces cerevisiae
Nat. Struct. Biol.
7
238-244
2000
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246394
Morbach
-
Engineering the homoserine deh ...
Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
45
612-620
1996
-
-
-
-
1
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246395
Pavagi
Purification and characterizat ...
Spinacia oleracea
Biochem. Mol. Biol. Int.
36
649-658
1995
1
-
-
-
-
-
7
3
-
-
2
-
-
2
-
-
1
-
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
7
-
3
-
-
2
-
-
-
-
1
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246387
Wedler
Kinetic and regulatory mechani ...
Escherichia coli
J. Biol. Chem.
268
4880-4888
1993
-
-
-
-
-
-
1
4
-
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
4
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246403
Omori
Role of serine 352 in the allo ...
Serratia marcescens
J. Bacteriol.
175
959-965
1993
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246398
Hama
Inhibition of homoserine dehyd ...
Escherichia coli
J. Biochem.
109
604-608
1991
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246399
Yumoto
Rapid purification and charact ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
285
270-275
1991
-
-
-
-
-
-
2
-
-
-
2
-
-
6
-
-
1
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
1
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246397
Yamaki
The mechanism of antifungal ac ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
168
837-843
1990
-
-
-
-
-
-
1
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246400
Angeles
The kinetic mechanism of the b ...
Escherichia coli
Arch. Biochem. Biophys.
283
96-101
1990
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246383
Krishnaswamy
Use of monoclonal antibodies f ...
Zea mays
Arch. Biochem. Biophys.
246
250-262
1986
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
1
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246384
Krishnaswamy
Ligand-induced interconversion ...
Zea mays
Arch. Biochem. Biophys.
222
449-463
1983
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
1
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246382
Sainis
Localisation and characterisat ...
Hordeum vulgare, Pisum sativum
Planta
152
491-496
1981
-
-
-
-
-
-
4
7
4
-
4
2
-
5
-
-
2
-
-
2
-
-
6
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
4
-
-
-
-
4
-
7
4
-
4
2
-
-
-
2
-
2
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246386
Di Camelli
Comparison of sensitive and de ...
Zea mays
Plant Physiol.
65
176-183
1980
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246388
Grego
-
Comparison of homoserine dehyd ...
Pisum sativum, Ricinus communis, Triticum aestivum
Phytochemistry
19
1619-1623
1980
-
-
-
-
-
-
3
5
-
15
5
3
-
3
-
-
3
-
-
3
3
-
8
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
6
-
-
-
-
3
-
5
-
15
5
3
-
-
-
3
-
3
3
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246385
Walter
Isolation and characterization ...
Zea mays
J. Biol. Chem.
254
1349-1355
1979
-
-
-
-
-
-
1
4
-
-
5
-
-
2
-
-
1
-
-
1
2
1
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
4
-
-
5
-
-
-
-
1
-
1
2
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246389
Epstein
Homoserine dehydrogenase of Rh ...
Rhodospirillum rubrum
Eur. J. Biochem.
82
453-461
1978
-
-
-
-
-
-
1
-
-
-
3
-
-
2
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246390
Ogilvie
Reaction of Tris with aldehyde ...
Escherichia coli
Biochim. Biophys. Acta
445
525-536
1976
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246391
Aarnes
-
Threonine-sensitive aspartate ...
Pisum sativum
Phytochemistry
13
2717-2724
1974
-
-
-
-
-
-
3
2
-
-
-
-
-
1
-
-
1
-
-
1
-
1
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
3
-
2
-
-
-
-
-
-
-
1
-
1
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246392
Cavari
Properties of homoserine dehyd ...
Thermophilic bacterium
Biochim. Biophys. Acta
302
183-190
1973
-
-
-
-
-
-
4
1
-
5
-
-
-
1
-
-
1
-
-
-
-
-
2
-
1
1
-
-
1
1
-
2
-
-
-
-
-
-
2
-
-
-
-
4
-
1
-
5
-
-
-
-
-
1
-
-
-
-
2
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-
246393
Saiki
Studies on homoserine dehydrog ...
Thermus thermophilus
J. Biochem.
74
1239-1248
1973
-
-
-
-
-
-
1
1
-
2
-
-
-
2
-
-
1
-
-
-
-
-
2
-
1
-
3
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
2
-
-
-
-
-
1
-
-
-
-
2
-
1
-
3
-
1
-
-
-
-
-
-
-
-
-