BRENDA - Enzyme Database show

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
EC Number
Amino acid exchange
Commentary
Organism
2.7.1.39
H139L
mutant enzyme with diminished kinase activity and ATPase activity 150fold greater than that of the wild-type enzyme
Escherichia coli
2.7.1.39
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
2.7.1.39
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
2.7.1.39
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 55C
Escherichia coli
2.7.1.39
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
2.7.1.39
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
EC Number
Inhibitors
Commentary
Organism
Structure
2.7.1.39
(4R)-4-hydroxypentan-2-one
-
Escherichia coli
2.7.1.39
(p-hydroxyphenyl)-glyoxal
-
Escherichia coli
2.7.1.39
2-amino-3-(phosphonoethyl)thiopropionate
-
Escherichia coli
2.7.1.39
2-Amino-5-phosphonovalerate
-
Escherichia coli
2.7.1.39
2-amino-5-phosphovalerate
-
Escherichia coli
2.7.1.39
L-2-amino-5-hydroxyvalerate
substrate inhibition
Escherichia coli
2.7.1.39
L-Cys
-
Escherichia coli
2.7.1.39
L-Glutamic acid
-
Escherichia coli
2.7.1.39
L-homoserine
-
Escherichia coli
2.7.1.39
L-homoserine alpha-methyl ester
substrate inhibition
Escherichia coli
2.7.1.39
L-homoserine ethyl ester
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
Escherichia coli
2.7.1.39
L-homoserine isopropyl ester
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
Escherichia coli
2.7.1.39
L-homoserine n-propyl ester
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
Escherichia coli
2.7.1.39
L-norvaline
-
Escherichia coli
2.7.1.39
L-Thr
substrate inhibition
Escherichia coli
2.7.1.39
O-phospho-L-serine
-
Escherichia coli
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.7.1.39
0.11
-
ATP
mutant enzyme H202L
Escherichia coli
2.7.1.39
0.11
-
L-homoserine
mutant enzyme H202L
Escherichia coli
2.7.1.39
0.13
-
ATP
mutant enzyme R234H; wild-type enzyme
Escherichia coli
2.7.1.39
0.13
-
L-homoserine
mutant enzyme R234H
Escherichia coli
2.7.1.39
0.14
-
L-homoserine
wild-type enzyme
Escherichia coli
2.7.1.39
0.15
-
ATP
mutant enzyme H205Q
Escherichia coli
2.7.1.39
0.21
-
ATP
mutant enzyme R234L
Escherichia coli
2.7.1.39
0.28
-
L-aspartate beta-semialdehyde
wild-type enzyme
Escherichia coli
2.7.1.39
0.49
-
ATP
mutant enzyme H139L
Escherichia coli
2.7.1.39
0.88
-
ATP
mutant enzyme R234C
Escherichia coli
2.7.1.39
1.1
-
L-2-amino-5-hydroxyvalerate
wild-type enzyme
Escherichia coli
2.7.1.39
1.2
-
L-homoserine isopropyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
1.9
-
L-homoserine ethyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
2.5
-
L-homoserine
mutant enzyme H139L
Escherichia coli
2.7.1.39
3.5
-
L-homoserine n-propyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
3.7
-
L-homoserine
mutant enzyme H205Q
Escherichia coli
2.7.1.39
4.9
-
L-homoserine methyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
5.8
-
L-homoserine n-butyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
6.2
-
L-homoserine
mutant enzyme R234H
Escherichia coli
2.7.1.39
6.9
-
L-homoserine
wild-type enzyme
Escherichia coli
2.7.1.39
6.9
-
L-homoserine isobutyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
8.5
-
L-homoserine
mutant enzyme R234C
Escherichia coli
2.7.1.39
11.6
-
L-2-amino-1,4-butanediol
wild-type enzyme
Escherichia coli
2.7.1.39
31.8
-
D-homoserine
wild-type enzyme
Escherichia coli
2.7.1.39
40.1
-
L-homoserine
mutant enzyme R234L
Escherichia coli
2.7.1.39
58.2
-
L-homoserine
mutant enzyme H202L
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.7.1.39
ATP + L-homoserine
Escherichia coli
enzyme in the aspartate pathway of amino acid biosynthesis
ADP + O-phospho-L-homoserine
-
Escherichia coli
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.7.1.39
Escherichia coli
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.7.1.39
ATP + D-homoserine
32% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-D-homoserine
-
-
-
?
2.7.1.39
ATP + L-2-amino-1,4-butanediol
7.9% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + ?
-
-
-
?
2.7.1.39
ATP + L-2-amino-5-hydroxyvalerate
9.9% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + L-2-amino-5-phosphovalerate
-
-
-
?
2.7.1.39
ATP + L-aspartate 4-semialdehyde
8.2% of the turnover number with L-homoserine
641471
Escherichia coli
?
-
-
-
?
2.7.1.39
ATP + L-homoserine
-
641471
Escherichia coli
ADP + O-phospho-L-homoserine
-
641471
Escherichia coli
?
2.7.1.39
ATP + L-homoserine
enzyme in the aspartate pathway of amino acid biosynthesis
641471
Escherichia coli
ADP + O-phospho-L-homoserine
-
641471
Escherichia coli
?
2.7.1.39
ATP + L-homoserine ethyl ester
74% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine ethyl ester
-
-
-
?
2.7.1.39
ATP + L-homoserine isopropyl ester
74% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine isopropyl ester
-
-
-
?
2.7.1.39
ATP + L-homoserine isubutyl ester
84% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine isobutyl ester
-
-
-
?
2.7.1.39
ATP + L-homoserine methyl ester
80% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine methyl ester
-
-
-
?
2.7.1.39
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
-
-
-
?
2.7.1.39
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
-
-
-
?
2.7.1.39
additional information
enzyme has inherent ATPase activity
641471
Escherichia coli
?
-
-
-
-
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.7.1.39
0.007
-
L-homoserine butyl ester
mutant R234L
Escherichia coli
2.7.1.39
0.0111
-
L-homoserine propyl ester
mutant R234L
Escherichia coli
2.7.1.39
0.018
-
L-homoserine methyl ester
mutant R234L
Escherichia coli
2.7.1.39
0.021
-
L-homoserine ethyl ester
mutant R234L
Escherichia coli
2.7.1.39
0.2
-
L-homoserine
mutant R234L
Escherichia coli
2.7.1.39
2
-
L-2-amino-1,4-butanediol
wild-type enzyme
Escherichia coli
2.7.1.39
2.1
-
L-aspartate beta-semialdehyde
wild-type enzyme
Escherichia coli
2.7.1.39
2.5
-
L-2-amino-5-hydroxyvalerate
wild-type enzyme
Escherichia coli
2.7.1.39
2.5
-
L-homoserine butyl ester
mutant H202L
Escherichia coli
2.7.1.39
2.7
-
L-homoserine propyl ester
mutant H202L
Escherichia coli
2.7.1.39
3.3
-
D-homoserine
wild-type enzyme
Escherichia coli
2.7.1.39
4.1
-
L-homoserine ethyl ester
mutant H202L
Escherichia coli
2.7.1.39
5.4
-
L-homoserine methyl ester
mutant H202L
Escherichia coli
2.7.1.39
9.1
-
L-homoserine
mutant H202L
Escherichia coli
2.7.1.39
13.6
-
L-homoserine ethyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
13.6
-
L-homoserine isopropyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
14
-
L-homoserine n-propyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
14.7
-
L-homoserine methyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
16.4
-
L-homoserine isobutyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
18.3
-
L-homoserine
wild-type enzyme
Escherichia coli
2.7.1.39
29.1
-
L-homoserine n-butyl ester
wild-type enzyme
Escherichia coli
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.7.1.39
8
-
wild-type enzyme
Escherichia coli
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
2.7.1.39
0.2
0.5
(4R)-4-hydroxypentan-2-one
wild-type enzyme
Escherichia coli
2.7.1.39
0.2
0.5
L-Glutamic acid
wild-type enzyme
Escherichia coli
2.7.1.39
0.2
0.5
L-norvaline
wild-type enzyme
Escherichia coli
2.7.1.39
0.3
-
2-amino-3-(phosphonoethyl)thiopropionate
wild-type enzyme
Escherichia coli
2.7.1.39
0.3
-
L-Thr
wild-type enzyme
Escherichia coli
2.7.1.39
0.46
-
L-Cys
wild-type enzyme
Escherichia coli
2.7.1.39
2.7
-
O-phospho-L-serine
-
Escherichia coli
2.7.1.39
10.4
-
2-amino-5-phosphovalerate
-
Escherichia coli
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
2.7.1.39
H139L
mutant enzyme with diminished kinase activity and ATPase activity 150fold greater than that of the wild-type enzyme
Escherichia coli
2.7.1.39
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
2.7.1.39
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
2.7.1.39
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 55C
Escherichia coli
2.7.1.39
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
2.7.1.39
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)
EC Number
Inhibitors
Commentary
Organism
Structure
2.7.1.39
(4R)-4-hydroxypentan-2-one
-
Escherichia coli
2.7.1.39
(p-hydroxyphenyl)-glyoxal
-
Escherichia coli
2.7.1.39
2-amino-3-(phosphonoethyl)thiopropionate
-
Escherichia coli
2.7.1.39
2-Amino-5-phosphonovalerate
-
Escherichia coli
2.7.1.39
2-amino-5-phosphovalerate
-
Escherichia coli
2.7.1.39
L-2-amino-5-hydroxyvalerate
substrate inhibition
Escherichia coli
2.7.1.39
L-Cys
-
Escherichia coli
2.7.1.39
L-Glutamic acid
-
Escherichia coli
2.7.1.39
L-homoserine
-
Escherichia coli
2.7.1.39
L-homoserine alpha-methyl ester
substrate inhibition
Escherichia coli
2.7.1.39
L-homoserine ethyl ester
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
Escherichia coli
2.7.1.39
L-homoserine isopropyl ester
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
Escherichia coli
2.7.1.39
L-homoserine n-propyl ester
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
Escherichia coli
2.7.1.39
L-norvaline
-
Escherichia coli
2.7.1.39
L-Thr
substrate inhibition
Escherichia coli
2.7.1.39
O-phospho-L-serine
-
Escherichia coli
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
2.7.1.39
0.2
0.5
(4R)-4-hydroxypentan-2-one
wild-type enzyme
Escherichia coli
2.7.1.39
0.2
0.5
L-Glutamic acid
wild-type enzyme
Escherichia coli
2.7.1.39
0.2
0.5
L-norvaline
wild-type enzyme
Escherichia coli
2.7.1.39
0.3
-
2-amino-3-(phosphonoethyl)thiopropionate
wild-type enzyme
Escherichia coli
2.7.1.39
0.3
-
L-Thr
wild-type enzyme
Escherichia coli
2.7.1.39
0.46
-
L-Cys
wild-type enzyme
Escherichia coli
2.7.1.39
2.7
-
O-phospho-L-serine
-
Escherichia coli
2.7.1.39
10.4
-
2-amino-5-phosphovalerate
-
Escherichia coli
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.7.1.39
0.11
-
ATP
mutant enzyme H202L
Escherichia coli
2.7.1.39
0.11
-
L-homoserine
mutant enzyme H202L
Escherichia coli
2.7.1.39
0.13
-
ATP
mutant enzyme R234H; wild-type enzyme
Escherichia coli
2.7.1.39
0.13
-
L-homoserine
mutant enzyme R234H
Escherichia coli
2.7.1.39
0.14
-
L-homoserine
wild-type enzyme
Escherichia coli
2.7.1.39
0.15
-
ATP
mutant enzyme H205Q
Escherichia coli
2.7.1.39
0.21
-
ATP
mutant enzyme R234L
Escherichia coli
2.7.1.39
0.28
-
L-aspartate beta-semialdehyde
wild-type enzyme
Escherichia coli
2.7.1.39
0.49
-
ATP
mutant enzyme H139L
Escherichia coli
2.7.1.39
0.88
-
ATP
mutant enzyme R234C
Escherichia coli
2.7.1.39
1.1
-
L-2-amino-5-hydroxyvalerate
wild-type enzyme
Escherichia coli
2.7.1.39
1.2
-
L-homoserine isopropyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
1.9
-
L-homoserine ethyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
2.5
-
L-homoserine
mutant enzyme H139L
Escherichia coli
2.7.1.39
3.5
-
L-homoserine n-propyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
3.7
-
L-homoserine
mutant enzyme H205Q
Escherichia coli
2.7.1.39
4.9
-
L-homoserine methyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
5.8
-
L-homoserine n-butyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
6.2
-
L-homoserine
mutant enzyme R234H
Escherichia coli
2.7.1.39
6.9
-
L-homoserine
wild-type enzyme
Escherichia coli
2.7.1.39
6.9
-
L-homoserine isobutyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
8.5
-
L-homoserine
mutant enzyme R234C
Escherichia coli
2.7.1.39
11.6
-
L-2-amino-1,4-butanediol
wild-type enzyme
Escherichia coli
2.7.1.39
31.8
-
D-homoserine
wild-type enzyme
Escherichia coli
2.7.1.39
40.1
-
L-homoserine
mutant enzyme R234L
Escherichia coli
2.7.1.39
58.2
-
L-homoserine
mutant enzyme H202L
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.7.1.39
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)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.7.1.39
ATP + D-homoserine
32% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-D-homoserine
-
-
-
?
2.7.1.39
ATP + L-2-amino-1,4-butanediol
7.9% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + ?
-
-
-
?
2.7.1.39
ATP + L-2-amino-5-hydroxyvalerate
9.9% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + L-2-amino-5-phosphovalerate
-
-
-
?
2.7.1.39
ATP + L-aspartate 4-semialdehyde
8.2% of the turnover number with L-homoserine
641471
Escherichia coli
?
-
-
-
?
2.7.1.39
ATP + L-homoserine
-
641471
Escherichia coli
ADP + O-phospho-L-homoserine
-
641471
Escherichia coli
?
2.7.1.39
ATP + L-homoserine
enzyme in the aspartate pathway of amino acid biosynthesis
641471
Escherichia coli
ADP + O-phospho-L-homoserine
-
641471
Escherichia coli
?
2.7.1.39
ATP + L-homoserine ethyl ester
74% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine ethyl ester
-
-
-
?
2.7.1.39
ATP + L-homoserine isopropyl ester
74% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine isopropyl ester
-
-
-
?
2.7.1.39
ATP + L-homoserine isubutyl ester
84% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine isobutyl ester
-
-
-
?
2.7.1.39
ATP + L-homoserine methyl ester
80% of the turnover number with L-homoserine
641471
Escherichia coli
ADP + O-phospho-L-homoserine methyl ester
-
-
-
?
2.7.1.39
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
-
-
-
?
2.7.1.39
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
-
-
-
?
2.7.1.39
additional information
enzyme has inherent ATPase activity
641471
Escherichia coli
?
-
-
-
-
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.7.1.39
0.007
-
L-homoserine butyl ester
mutant R234L
Escherichia coli
2.7.1.39
0.0111
-
L-homoserine propyl ester
mutant R234L
Escherichia coli
2.7.1.39
0.018
-
L-homoserine methyl ester
mutant R234L
Escherichia coli
2.7.1.39
0.021
-
L-homoserine ethyl ester
mutant R234L
Escherichia coli
2.7.1.39
0.2
-
L-homoserine
mutant R234L
Escherichia coli
2.7.1.39
2
-
L-2-amino-1,4-butanediol
wild-type enzyme
Escherichia coli
2.7.1.39
2.1
-
L-aspartate beta-semialdehyde
wild-type enzyme
Escherichia coli
2.7.1.39
2.5
-
L-2-amino-5-hydroxyvalerate
wild-type enzyme
Escherichia coli
2.7.1.39
2.5
-
L-homoserine butyl ester
mutant H202L
Escherichia coli
2.7.1.39
2.7
-
L-homoserine propyl ester
mutant H202L
Escherichia coli
2.7.1.39
3.3
-
D-homoserine
wild-type enzyme
Escherichia coli
2.7.1.39
4.1
-
L-homoserine ethyl ester
mutant H202L
Escherichia coli
2.7.1.39
5.4
-
L-homoserine methyl ester
mutant H202L
Escherichia coli
2.7.1.39
9.1
-
L-homoserine
mutant H202L
Escherichia coli
2.7.1.39
13.6
-
L-homoserine ethyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
13.6
-
L-homoserine isopropyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
14
-
L-homoserine n-propyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
14.7
-
L-homoserine methyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
16.4
-
L-homoserine isobutyl ester
wild-type enzyme
Escherichia coli
2.7.1.39
18.3
-
L-homoserine
wild-type enzyme
Escherichia coli
2.7.1.39
29.1
-
L-homoserine n-butyl ester
wild-type enzyme
Escherichia coli
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.7.1.39
8
-
wild-type enzyme
Escherichia coli