BRENDA - Enzyme Database show

Role of arginine 138 in the catalysis and regulation of Escherichia coli dihydrodipicolinate synthase

Dobson, R.C.; Devenish, S.R.; Turner, L.A.; Clifford, V.R.; Pearce, F.G.; Jameson, G.B.; Gerrard, J.A.; Biochemistry 44, 13007-13013 (2005)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
4.3.3.7
crystal structure of mutant enzyme R138H and R138A, hanging-drop vapor diffusion method
Escherichia coli
Engineering
EC Number
Amino acid exchange
Commentary
Organism
4.3.3.7
R138A
activity is approximately 0.1% of wild-type activity, Km-value for L-aspartate 4-semialdehyde is significantly higher than the wild-type value, shows the same IC50 values as the wild-type enzyme, but different partial inhibition patterns
Escherichia coli
4.3.3.7
R138H
activity is approximately 0.1% of wild-type activity, Km-value for L-aspartate 4-semialdehyde is significantly higher than the wild-type value, shows the same IC50 values as the wild-type enzyme, but different partial inhibition patterns
Escherichia coli
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
(S)-lysine
mutant enzymes R138H and R138A show the same IC50 values as the wild-type enzyme, but different partial inhibition patterns
Escherichia coli
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.3.3.7
0.28
-
pyruvate
mutant enzyme R138H
Escherichia coli
4.3.3.7
0.45
-
pyruvate
mutant enzyme R138A
Escherichia coli
4.3.3.7
5.1
-
L-aspartate 4-semialdehyde
mutant enzyme R138A
Escherichia coli
4.3.3.7
37
-
L-aspartate 4-semialdehyde
mutant enzyme R138H
Escherichia coli
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.3.3.7
31000
-
x * 31000, SDS-PAGE
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.3.3.7
L-aspartate 4-semialdehyde + pyruvate
Escherichia coli
-
dihydrodipicolinate + H2O
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.3.3.7
Escherichia coli
P0A6L2
-
-
Purification (Commentary)
EC Number
Commentary
Organism
4.3.3.7
-
Escherichia coli
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
L-aspartate 4-semialdehyde + pyruvate
-
664072
Escherichia coli
dihydrodipicolinate + H2O
-
-
-
?
4.3.3.7
L-aspartate 4-semialdehyde + pyruvate
branch poit of (S)-lysine biosynthesis
664072
Escherichia coli
dihydrodipicolinate + H2O
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
4.3.3.7
?
x * 31000, SDS-PAGE
Escherichia coli
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.3.3.7
0.038
-
L-aspartate 4-semialdehyde
mutant enzyme R138H
Escherichia coli
4.3.3.7
0.038
-
pyruvate
mutant enzyme R138H
Escherichia coli
4.3.3.7
0.149
-
L-aspartate 4-semialdehyde
mutant enzyme R138A
Escherichia coli
4.3.3.7
0.149
-
pyruvate
mutant enzyme R138A
Escherichia coli
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.3.3.7
crystal structure of mutant enzyme R138H and R138A, hanging-drop vapor diffusion method
Escherichia coli
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
4.3.3.7
R138A
activity is approximately 0.1% of wild-type activity, Km-value for L-aspartate 4-semialdehyde is significantly higher than the wild-type value, shows the same IC50 values as the wild-type enzyme, but different partial inhibition patterns
Escherichia coli
4.3.3.7
R138H
activity is approximately 0.1% of wild-type activity, Km-value for L-aspartate 4-semialdehyde is significantly higher than the wild-type value, shows the same IC50 values as the wild-type enzyme, but different partial inhibition patterns
Escherichia coli
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
(S)-lysine
mutant enzymes R138H and R138A show the same IC50 values as the wild-type enzyme, but different partial inhibition patterns
Escherichia coli
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.3.3.7
0.28
-
pyruvate
mutant enzyme R138H
Escherichia coli
4.3.3.7
0.45
-
pyruvate
mutant enzyme R138A
Escherichia coli
4.3.3.7
5.1
-
L-aspartate 4-semialdehyde
mutant enzyme R138A
Escherichia coli
4.3.3.7
37
-
L-aspartate 4-semialdehyde
mutant enzyme R138H
Escherichia coli
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.3.3.7
31000
-
x * 31000, SDS-PAGE
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
4.3.3.7
L-aspartate 4-semialdehyde + pyruvate
Escherichia coli
-
dihydrodipicolinate + H2O
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.3.3.7
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
L-aspartate 4-semialdehyde + pyruvate
-
664072
Escherichia coli
dihydrodipicolinate + H2O
-
-
-
?
4.3.3.7
L-aspartate 4-semialdehyde + pyruvate
branch poit of (S)-lysine biosynthesis
664072
Escherichia coli
dihydrodipicolinate + H2O
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.3.3.7
?
x * 31000, SDS-PAGE
Escherichia coli
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.3.3.7
0.038
-
L-aspartate 4-semialdehyde
mutant enzyme R138H
Escherichia coli
4.3.3.7
0.038
-
pyruvate
mutant enzyme R138H
Escherichia coli
4.3.3.7
0.149
-
L-aspartate 4-semialdehyde
mutant enzyme R138A
Escherichia coli
4.3.3.7
0.149
-
pyruvate
mutant enzyme R138A
Escherichia coli