Application | Comment | Organism |
---|---|---|
drug development | the allosteric binding site of DHDPS may be a good starting point for development of an inhibitor specific to Neisseria meningitidis | Neisseria meningitidis |
Cloned (Comment) | Organism |
---|---|
as His-tagged constructs | Escherichia coli |
into the expression vector pET151-D to give the plasmid pFH02, to transform chemically super-competent Escherichia coli Top10 cells | Neisseria meningitidis |
Crystallization (Comment) | Organism |
---|---|
to 2.0 A resolution, space group of the crystal is P212121, with unit cell dimensions of a = 80.7, b = 115.7 and c = 132.1 A. The secondary and tertiary structures are remarkably similar to that of Escherichia coli DHDPS. The hydrogen bond lengths within the catalytic triad, and particularly that between Y133 and T44, differ significantly from those of the Escherichia coli enzyme | Neisseria meningitidis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-aspartate 4-semialdehyde | is subject to substrate inhibition by high concentrations | Neisseria meningitidis | |
L-lysine | - |
Escherichia coli | |
L-lysine | is significantly more sensitive to feedback inhibition than Escherichia coli DHDPS | Neisseria meningitidis | |
additional information | no substrate inhibition by (S)-aspartate 4-semialdehyde | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.052 | - |
L-aspartate 4-semialdehyde | at 30°C, in 100 mM HEPES buffer, pH 8.0 | Neisseria meningitidis | |
0.11 | - |
L-aspartate 4-semialdehyde | at 30°C, in 100 mM HEPES buffer, pH 8.0 | Escherichia coli | |
0.26 | - |
pyruvate | at 30°C, in 100 mM HEPES buffer, pH 8.0 | Escherichia coli | |
0.5 | - |
pyruvate | at 30°C, in 100 mM HEPES buffer, pH 8.0 | Neisseria meningitidis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
31510 | - |
mass spectrometry | Neisseria meningitidis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Neisseria meningitidis | Q9JZR4 | - |
- |
Neisseria meningitidis MC58 | Q9JZR4 | - |
- |
Purification (Comment) | Organism |
---|---|
by centrifugation and gel filtration | Escherichia coli |
by centrifugation and gel filtration, to homogeneity | Neisseria meningitidis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate 4-semialdehyde + pyruvate | - |
Escherichia coli | dihydrodipicolinate + 2 H2O | - |
? | |
L-aspartate 4-semialdehyde + pyruvate | slightly higher affinity for L-aspartate 4-semialdehyde and somewhat lower affinity for pyruvate than the Escherichia coli enzyme, whereby the catalytic activity is similar | Neisseria meningitidis | dihydrodipicolinate + 2 H2O | - |
? | |
L-aspartate 4-semialdehyde + pyruvate | slightly higher affinity for L-aspartate 4-semialdehyde and somewhat lower affinity for pyruvate than the Escherichia coli enzyme, whereby the catalytic activity is similar | Neisseria meningitidis MC58 | dihydrodipicolinate + 2 H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | crystallography | Neisseria meningitidis |
Synonyms | Comment | Organism |
---|---|---|
DapA | - |
Escherichia coli |
DapA | - |
Neisseria meningitidis |
DHDPS | - |
Escherichia coli |
DHDPS | - |
Neisseria meningitidis |
dihydrodipicolinate synthase | - |
Escherichia coli |
dihydrodipicolinate synthase | - |
Neisseria meningitidis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
46.5 | - |
melting temperature in the absence of substrates | Neisseria meningitidis |
59.5 | - |
melting temperature in the absence of substrates | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
46.7 | - |
pyruvate | at 30°C, in 100 mM HEPES buffer, pH 8.0 | Neisseria meningitidis | |
124 | - |
pyruvate | at 30°C, in 100 mM HEPES buffer, pH 8.0 | Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.058 | - |
L-lysine | with (S)-aspartate 4-semialdehyde as substrate | Neisseria meningitidis | |
0.32 | - |
L-lysine | with (S)-aspartate 4-semialdehyde as substrate | Escherichia coli | |
1.7 | - |
L-lysine | with pyruvate as substrate | Neisseria meningitidis | |
3.9 | - |
L-lysine | with pyruvate as substrate | Escherichia coli |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.053 | - |
- |
Neisseria meningitidis | L-lysine |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
93.4 | - |
pyruvate | at 30°C, in 100 mM HEPES buffer, pH 8.0 | Neisseria meningitidis | |
898 | - |
L-aspartate 4-semialdehyde | at 30°C, in 100 mM HEPES buffer, pH 8.0 | Neisseria meningitidis |