BRENDA - Enzyme Database show
show all sequences of 2.7.1.39

Substrate specificity and identification of functional groups of homoserine kinase from Escherichia coli

Huo, X.; Viola, R.E.; Biochemistry 35, 16180-16185 (1996)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
H139L
mutant enzyme with diminished kinase activity and ATPase activity 150fold greater than that of the wild-type enzyme
Escherichia coli
H202L
Km-value for L-homoserine and ATP remain unchanged, the Ki-value for substrate inhibition by L-homoserine increases about 8fold, the turnover-number decreases by 50%,unlike the wild-type enzyme the L-homoserine ethyl, isopropyl, and n-propyl esters show substrate inhibition
Escherichia coli
H205Q
Km-value for ATP remains unchanged, ATPase activity is within a factor 2 of the wild-type enzyme, the kinase activity is less than 0.03% that of the wild-type enzyme
Escherichia coli
R234C
no observable homoserine kinase activity, the ATPase activity is nearly 20 times that of the wild-type enzyme at pH 8.0. 7fold increase in Km-value for ATP. Mutant enzyme is sensitive to heat treatment and begins to precipitate at 55°C
Escherichia coli
R234H
mutant enzyme has a diminished kinase activity, 0.4% of that of the wild-type enzyme, and an enhanced ATPase activity, Km-values for both substrates are unchanged
Escherichia coli
R234L
Km-value for L-homoserine increases nearly 300fold, the turnover-number decreases by 90fold compared to the wild-type enzyme. Less than a 2fold change in Km for ATP, the inherent ATPase activity increases by 3fold. The mutant enzyme has turnover-numbers for homoserine esters that are only 10% that of homoserine, but has higher affinity for the esters than for L-homoserine itself. L-Cys, a strong inhibitor of the wild-type enzyme, is 50fold less effective as inhibitor of the mutant enzyme. L-Thr no longer inhibits the mutant enzyme. Unlike the wild-type enzyme, addition of 10 mM L-homoserine to the mutant enzyme has no protective effect on the number of arginyl residues titrated with (p-hydroxyphenyl)glyoxal
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
(4R)-4-hydroxypentan-2-one
-
Escherichia coli
(p-hydroxyphenyl)-glyoxal
-
Escherichia coli
2-amino-3-(phosphonoethyl)thiopropionate
-
Escherichia coli
2-Amino-5-phosphonovalerate
-
Escherichia coli
2-amino-5-phosphovalerate
-
Escherichia coli
L-2-amino-5-hydroxyvalerate
substrate inhibition
Escherichia coli
L-Cys
-
Escherichia coli
L-Glutamic acid
-
Escherichia coli
L-homoserine
-
Escherichia coli
L-homoserine alpha-methyl ester
substrate inhibition
Escherichia coli
L-homoserine ethyl ester
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
Escherichia coli
L-homoserine isopropyl ester
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
Escherichia coli
L-homoserine n-propyl ester
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
Escherichia coli
L-norvaline
-
Escherichia coli
L-Thr
substrate inhibition
Escherichia coli
O-phospho-L-serine
-
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.11
-
ATP
mutant enzyme H202L
Escherichia coli
0.11
-
L-homoserine
mutant enzyme H202L
Escherichia coli
0.13
-
ATP
mutant enzyme R234H; wild-type enzyme
Escherichia coli
0.13
-
L-homoserine
mutant enzyme R234H
Escherichia coli
0.14
-
L-homoserine
wild-type enzyme
Escherichia coli
0.15
-
ATP
mutant enzyme H205Q
Escherichia coli
0.21
-
ATP
mutant enzyme R234L
Escherichia coli
0.28
-
L-aspartate beta-semialdehyde
wild-type enzyme
Escherichia coli
0.49
-
ATP
mutant enzyme H139L
Escherichia coli
0.88
-
ATP
mutant enzyme R234C
Escherichia coli
1.1
-
L-2-amino-5-hydroxyvalerate
wild-type enzyme
Escherichia coli
1.2
-
L-homoserine isopropyl ester
wild-type enzyme
Escherichia coli
1.9
-
L-homoserine ethyl ester
wild-type enzyme
Escherichia coli
2.5
-
L-homoserine
mutant enzyme H139L
Escherichia coli
3.5
-
L-homoserine n-propyl ester
wild-type enzyme
Escherichia coli
3.7
-
L-homoserine
mutant enzyme H205Q
Escherichia coli
4.9
-
L-homoserine methyl ester
wild-type enzyme
Escherichia coli
5.8
-
L-homoserine n-butyl ester
wild-type enzyme
Escherichia coli
6.2
-
L-homoserine
mutant enzyme R234H
Escherichia coli
6.9
-
L-homoserine
wild-type enzyme
Escherichia coli
6.9
-
L-homoserine isobutyl ester
wild-type enzyme
Escherichia coli
8.5
-
L-homoserine
mutant enzyme R234C
Escherichia coli
11.6
-
L-2-amino-1,4-butanediol
wild-type enzyme
Escherichia coli
31.8
-
D-homoserine
wild-type enzyme
Escherichia coli
40.1
-
L-homoserine
mutant enzyme R234L
Escherichia coli
58.2
-
L-homoserine
mutant enzyme H202L
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-homoserine
Escherichia coli
enzyme in the aspartate pathway of amino acid biosynthesis
ADP + O-phospho-L-homoserine
-
Escherichia coli
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + D-homoserine
32% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-D-homoserine
-
-
-
?
ATP + L-2-amino-1,4-butanediol
7.9% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + ?
-
-
-
?
ATP + L-2-amino-5-hydroxyvalerate
9.9% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + L-2-amino-5-phosphovalerate
-
-
-
?
ATP + L-aspartate 4-semialdehyde
8.2% of the turnover number with L-homoserine
641471
Escherichia coli
?
-
-
-
?
ATP + L-homoserine
-
641471
Escherichia coli
ADP + O-phospho-L-homoserine
-
641471
Escherichia coli
?
ATP + L-homoserine
enzyme in the aspartate pathway of amino acid biosynthesis
641471
Escherichia coli
ADP + O-phospho-L-homoserine
-
641471
Escherichia coli
?
ATP + L-homoserine ethyl ester
74% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine ethyl ester
-
-
-
?
ATP + L-homoserine isopropyl ester
74% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine isopropyl ester
-
-
-
?
ATP + L-homoserine isubutyl ester
84% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine isobutyl ester
-
-
-
?
ATP + L-homoserine methyl ester
80% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine methyl ester
-
-
-
?
ATP + L-homoserine n-butyl ester
160% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine n-butyl ester
-
-
-
?
ATP + L-homoserine n-propyl ester
76% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine n-propyl ester
-
-
-
?
additional information
enzyme has inherent ATPase activity
641471
Escherichia coli
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.007
-
L-homoserine butyl ester
mutant R234L
Escherichia coli
0.0111
-
L-homoserine propyl ester
mutant R234L
Escherichia coli
0.018
-
L-homoserine methyl ester
mutant R234L
Escherichia coli
0.021
-
L-homoserine ethyl ester
mutant R234L
Escherichia coli
0.2
-
L-homoserine
mutant R234L
Escherichia coli
2
-
L-2-amino-1,4-butanediol
wild-type enzyme
Escherichia coli
2.1
-
L-aspartate beta-semialdehyde
wild-type enzyme
Escherichia coli
2.5
-
L-2-amino-5-hydroxyvalerate
wild-type enzyme
Escherichia coli
2.5
-
L-homoserine butyl ester
mutant H202L
Escherichia coli
2.7
-
L-homoserine propyl ester
mutant H202L
Escherichia coli
3.3
-
D-homoserine
wild-type enzyme
Escherichia coli
4.1
-
L-homoserine ethyl ester
mutant H202L
Escherichia coli
5.4
-
L-homoserine methyl ester
mutant H202L
Escherichia coli
9.1
-
L-homoserine
mutant H202L
Escherichia coli
13.6
-
L-homoserine ethyl ester
wild-type enzyme
Escherichia coli
13.6
-
L-homoserine isopropyl ester
wild-type enzyme
Escherichia coli
14
-
L-homoserine n-propyl ester
wild-type enzyme
Escherichia coli
14.7
-
L-homoserine methyl ester
wild-type enzyme
Escherichia coli
16.4
-
L-homoserine isobutyl ester
wild-type enzyme
Escherichia coli
18.3
-
L-homoserine
wild-type enzyme
Escherichia coli
29.1
-
L-homoserine n-butyl ester
wild-type enzyme
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
wild-type enzyme
Escherichia coli
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.2
0.5
(4R)-4-hydroxypentan-2-one
wild-type enzyme
Escherichia coli
0.2
0.5
L-Glutamic acid
wild-type enzyme
Escherichia coli
0.2
0.5
L-norvaline
wild-type enzyme
Escherichia coli
0.3
-
2-amino-3-(phosphonoethyl)thiopropionate
wild-type enzyme
Escherichia coli
0.3
-
L-Thr
wild-type enzyme
Escherichia coli
0.46
-
L-Cys
wild-type enzyme
Escherichia coli
2.7
-
O-phospho-L-serine
-
Escherichia coli
10.4
-
2-amino-5-phosphovalerate
-
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H139L
mutant enzyme with diminished kinase activity and ATPase activity 150fold greater than that of the wild-type enzyme
Escherichia coli
H202L
Km-value for L-homoserine and ATP remain unchanged, the Ki-value for substrate inhibition by L-homoserine increases about 8fold, the turnover-number decreases by 50%,unlike the wild-type enzyme the L-homoserine ethyl, isopropyl, and n-propyl esters show substrate inhibition
Escherichia coli
H205Q
Km-value for ATP remains unchanged, ATPase activity is within a factor 2 of the wild-type enzyme, the kinase activity is less than 0.03% that of the wild-type enzyme
Escherichia coli
R234C
no observable homoserine kinase activity, the ATPase activity is nearly 20 times that of the wild-type enzyme at pH 8.0. 7fold increase in Km-value for ATP. Mutant enzyme is sensitive to heat treatment and begins to precipitate at 55°C
Escherichia coli
R234H
mutant enzyme has a diminished kinase activity, 0.4% of that of the wild-type enzyme, and an enhanced ATPase activity, Km-values for both substrates are unchanged
Escherichia coli
R234L
Km-value for L-homoserine increases nearly 300fold, the turnover-number decreases by 90fold compared to the wild-type enzyme. Less than a 2fold change in Km for ATP, the inherent ATPase activity increases by 3fold. The mutant enzyme has turnover-numbers for homoserine esters that are only 10% that of homoserine, but has higher affinity for the esters than for L-homoserine itself. L-Cys, a strong inhibitor of the wild-type enzyme, is 50fold less effective as inhibitor of the mutant enzyme. L-Thr no longer inhibits the mutant enzyme. Unlike the wild-type enzyme, addition of 10 mM L-homoserine to the mutant enzyme has no protective effect on the number of arginyl residues titrated with (p-hydroxyphenyl)glyoxal
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(4R)-4-hydroxypentan-2-one
-
Escherichia coli
(p-hydroxyphenyl)-glyoxal
-
Escherichia coli
2-amino-3-(phosphonoethyl)thiopropionate
-
Escherichia coli
2-Amino-5-phosphonovalerate
-
Escherichia coli
2-amino-5-phosphovalerate
-
Escherichia coli
L-2-amino-5-hydroxyvalerate
substrate inhibition
Escherichia coli
L-Cys
-
Escherichia coli
L-Glutamic acid
-
Escherichia coli
L-homoserine
-
Escherichia coli
L-homoserine alpha-methyl ester
substrate inhibition
Escherichia coli
L-homoserine ethyl ester
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
Escherichia coli
L-homoserine isopropyl ester
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
Escherichia coli
L-homoserine n-propyl ester
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
Escherichia coli
L-norvaline
-
Escherichia coli
L-Thr
substrate inhibition
Escherichia coli
O-phospho-L-serine
-
Escherichia coli
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.2
0.5
(4R)-4-hydroxypentan-2-one
wild-type enzyme
Escherichia coli
0.2
0.5
L-Glutamic acid
wild-type enzyme
Escherichia coli
0.2
0.5
L-norvaline
wild-type enzyme
Escherichia coli
0.3
-
2-amino-3-(phosphonoethyl)thiopropionate
wild-type enzyme
Escherichia coli
0.3
-
L-Thr
wild-type enzyme
Escherichia coli
0.46
-
L-Cys
wild-type enzyme
Escherichia coli
2.7
-
O-phospho-L-serine
-
Escherichia coli
10.4
-
2-amino-5-phosphovalerate
-
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.11
-
ATP
mutant enzyme H202L
Escherichia coli
0.11
-
L-homoserine
mutant enzyme H202L
Escherichia coli
0.13
-
ATP
mutant enzyme R234H; wild-type enzyme
Escherichia coli
0.13
-
L-homoserine
mutant enzyme R234H
Escherichia coli
0.14
-
L-homoserine
wild-type enzyme
Escherichia coli
0.15
-
ATP
mutant enzyme H205Q
Escherichia coli
0.21
-
ATP
mutant enzyme R234L
Escherichia coli
0.28
-
L-aspartate beta-semialdehyde
wild-type enzyme
Escherichia coli
0.49
-
ATP
mutant enzyme H139L
Escherichia coli
0.88
-
ATP
mutant enzyme R234C
Escherichia coli
1.1
-
L-2-amino-5-hydroxyvalerate
wild-type enzyme
Escherichia coli
1.2
-
L-homoserine isopropyl ester
wild-type enzyme
Escherichia coli
1.9
-
L-homoserine ethyl ester
wild-type enzyme
Escherichia coli
2.5
-
L-homoserine
mutant enzyme H139L
Escherichia coli
3.5
-
L-homoserine n-propyl ester
wild-type enzyme
Escherichia coli
3.7
-
L-homoserine
mutant enzyme H205Q
Escherichia coli
4.9
-
L-homoserine methyl ester
wild-type enzyme
Escherichia coli
5.8
-
L-homoserine n-butyl ester
wild-type enzyme
Escherichia coli
6.2
-
L-homoserine
mutant enzyme R234H
Escherichia coli
6.9
-
L-homoserine
wild-type enzyme
Escherichia coli
6.9
-
L-homoserine isobutyl ester
wild-type enzyme
Escherichia coli
8.5
-
L-homoserine
mutant enzyme R234C
Escherichia coli
11.6
-
L-2-amino-1,4-butanediol
wild-type enzyme
Escherichia coli
31.8
-
D-homoserine
wild-type enzyme
Escherichia coli
40.1
-
L-homoserine
mutant enzyme R234L
Escherichia coli
58.2
-
L-homoserine
mutant enzyme H202L
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-homoserine
Escherichia coli
enzyme in the aspartate pathway of amino acid biosynthesis
ADP + O-phospho-L-homoserine
-
Escherichia coli
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + D-homoserine
32% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-D-homoserine
-
-
-
?
ATP + L-2-amino-1,4-butanediol
7.9% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + ?
-
-
-
?
ATP + L-2-amino-5-hydroxyvalerate
9.9% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + L-2-amino-5-phosphovalerate
-
-
-
?
ATP + L-aspartate 4-semialdehyde
8.2% of the turnover number with L-homoserine
641471
Escherichia coli
?
-
-
-
?
ATP + L-homoserine
-
641471
Escherichia coli
ADP + O-phospho-L-homoserine
-
641471
Escherichia coli
?
ATP + L-homoserine
enzyme in the aspartate pathway of amino acid biosynthesis
641471
Escherichia coli
ADP + O-phospho-L-homoserine
-
641471
Escherichia coli
?
ATP + L-homoserine ethyl ester
74% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine ethyl ester
-
-
-
?
ATP + L-homoserine isopropyl ester
74% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine isopropyl ester
-
-
-
?
ATP + L-homoserine isubutyl ester
84% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine isobutyl ester
-
-
-
?
ATP + L-homoserine methyl ester
80% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine methyl ester
-
-
-
?
ATP + L-homoserine n-butyl ester
160% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine n-butyl ester
-
-
-
?
ATP + L-homoserine n-propyl ester
76% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine n-propyl ester
-
-
-
?
additional information
enzyme has inherent ATPase activity
641471
Escherichia coli
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.007
-
L-homoserine butyl ester
mutant R234L
Escherichia coli
0.0111
-
L-homoserine propyl ester
mutant R234L
Escherichia coli
0.018
-
L-homoserine methyl ester
mutant R234L
Escherichia coli
0.021
-
L-homoserine ethyl ester
mutant R234L
Escherichia coli
0.2
-
L-homoserine
mutant R234L
Escherichia coli
2
-
L-2-amino-1,4-butanediol
wild-type enzyme
Escherichia coli
2.1
-
L-aspartate beta-semialdehyde
wild-type enzyme
Escherichia coli
2.5
-
L-2-amino-5-hydroxyvalerate
wild-type enzyme
Escherichia coli
2.5
-
L-homoserine butyl ester
mutant H202L
Escherichia coli
2.7
-
L-homoserine propyl ester
mutant H202L
Escherichia coli
3.3
-
D-homoserine
wild-type enzyme
Escherichia coli
4.1
-
L-homoserine ethyl ester
mutant H202L
Escherichia coli
5.4
-
L-homoserine methyl ester
mutant H202L
Escherichia coli
9.1
-
L-homoserine
mutant H202L
Escherichia coli
13.6
-
L-homoserine ethyl ester
wild-type enzyme
Escherichia coli
13.6
-
L-homoserine isopropyl ester
wild-type enzyme
Escherichia coli
14
-
L-homoserine n-propyl ester
wild-type enzyme
Escherichia coli
14.7
-
L-homoserine methyl ester
wild-type enzyme
Escherichia coli
16.4
-
L-homoserine isobutyl ester
wild-type enzyme
Escherichia coli
18.3
-
L-homoserine
wild-type enzyme
Escherichia coli
29.1
-
L-homoserine n-butyl ester
wild-type enzyme
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
wild-type enzyme
Escherichia coli
Other publictions for EC 2.7.1.39
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)
737948
Brewer
Mutations in the Arabidopsis h ...
Arabidopsis thaliana
BMC Plant Biol.
14
317
2014
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1
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7
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1
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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 toxicity in Sacchar ...
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Kingsbury
Fungal homoserine kinase (thr1 ...
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Eukaryot. Cell
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The intrinsic reactivity of AT ...
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Downy mildew resistance in Ara ...
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Plant Cell
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690392
Rinder
Regulation of aspartate-derive ...
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Kingsbury
Threonine biosynthetic genes a ...
Cryptococcus neoformans
Microbiology
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Methionine and threonine synth ...
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Paik
Identification of virulence de ...
Streptococcus sanguinis, Streptococcus sanguinis SK36
Infect. Immun.
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661325
Bareich
Small molecule functional disc ...
Schizosaccharomyces pombe
Bioorg. Med. Chem.
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Role of homoserine and threoni ...
Streptomyces sp., Streptomyces sp. NRRL 5331
Microbiology
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Krishna
Structural basis for the catal ...
Methanocaldococcus jannaschii
Biochemistry
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2001
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Zhou
Structure and mechanism of hom ...
Methanocaldococcus jannaschii
Structure Fold. Des.
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2000
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Lee
Identification of the gene enc ...
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641476
Patte
ThrH, a homoserine kinase isoz ...
Pseudomonas aeruginosa
Microbiology
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1999
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Huo
Substrate specificity and iden ...
Escherichia coli
Biochemistry
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1996
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Huo
Functional group characterizat ...
Escherichia coli
Arch. Biochem. Biophys.
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641467
Riesmeier
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Purification to homogeneity an ...
Triticum aestivum
Phytochemistry
32
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641468
Ramos
Inhibition by different amino ...
Saccharomyces cerevisiae
FEBS Lett.
278
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1991
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Mannhaupt
Yeast homoserine kinase. Chara ...
Saccharomyces cerevisiae
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1990
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641464
Finkelnburg
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Homoserine kinase from phototr ...
Rhodospirillum rubrum, Rhodospirillum rubrum S1
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93-96
1987
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641463
Shames
Homoserine kinase of Escherich ...
Escherichia coli
Arch. Biochem. Biophys.
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1984
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641462
Baum
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Feedback inhibition of homoser ...
Raphanus sativus
Phytochemistry
22
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1983
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641461
Thoen
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Biosynthesis of threonine from ...
Pisum sativum
Plant Sci. Lett.
13
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641460
Aarnes
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Homoserine kinase from barley ...
Hordeum vulgare
Plant Sci. Lett.
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641470
Burr
Homoserine kinase from Escheri ...
Escherichia coli
Eur. J. Biochem.
62
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1976
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Theze
Homoserine kinase from Escheri ...
Escherichia coli
J. Bacteriol.
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Miyajima
Regulation of aspartate family ...
Brevibacterium flavum
J. Biochem.
71
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1972
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