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Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy

Blickling, S.; Renner, C.; Laber, B.; Pohlenz, H.; Holak, T.; Huber, R.; Biochemistry 36, 24-33 (1997)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
4.3.3.7
complexed with pyruvate, the substrate analogs succinate alpha-semialdehyde and alpa-ketopimelic acid, the inhibitor dipicolinic acid, and the natural feedback inhibitor L-lysine, hanging drop vapor diffusion method, in the presence of beta-octyl glucoside using either potassium phosphate buffer (pH 10) or potassium citrate buffer (pH 7.0) as the precipitant
Escherichia coli
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
2-oxopimelic acid
-
Escherichia coli
4.3.3.7
dipicolinic acid
-
Escherichia coli
4.3.3.7
L-lysine
natural feedback inhibitor
Escherichia coli
4.3.3.7
Succinate-semialdehyde
reversible inhibitor which is competitive with respect to L-aspartate-4-semialdehyde and uncompetitive with respect to pyruvate
Escherichia coli
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.3.3.7
Escherichia coli
P0A6L2
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
-
718827
Escherichia coli
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.3.3.7
0.17
-
2-oxopimelic acid
in 50 mM Tris-HCl (pH 8.2), at 22°C
Escherichia coli
4.3.3.7
0.3
-
Succinate-semialdehyde
in 50 mM Tris-HCl (pH 8.2), at 22°C
Escherichia coli
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.3.3.7
complexed with pyruvate, the substrate analogs succinate alpha-semialdehyde and alpa-ketopimelic acid, the inhibitor dipicolinic acid, and the natural feedback inhibitor L-lysine, hanging drop vapor diffusion method, in the presence of beta-octyl glucoside using either potassium phosphate buffer (pH 10) or potassium citrate buffer (pH 7.0) as the precipitant
Escherichia coli
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
2-oxopimelic acid
-
Escherichia coli
4.3.3.7
dipicolinic acid
-
Escherichia coli
4.3.3.7
L-lysine
natural feedback inhibitor
Escherichia coli
4.3.3.7
Succinate-semialdehyde
reversible inhibitor which is competitive with respect to L-aspartate-4-semialdehyde and uncompetitive with respect to pyruvate
Escherichia coli
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.3.3.7
0.17
-
2-oxopimelic acid
in 50 mM Tris-HCl (pH 8.2), at 22°C
Escherichia coli
4.3.3.7
0.3
-
Succinate-semialdehyde
in 50 mM Tris-HCl (pH 8.2), at 22°C
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
pyruvate + L-aspartate-4-semialdehyde
-
718827
Escherichia coli
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
General Information
EC Number
General Information
Commentary
Organism
4.3.3.7
metabolism
first enzyme unique to the diaminopimelate pathway of lysine biosynthesis
Escherichia coli
General Information (protein specific)
EC Number
General Information
Commentary
Organism
4.3.3.7
metabolism
first enzyme unique to the diaminopimelate pathway of lysine biosynthesis
Escherichia coli