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Literature summary for 4.3.3.7 extracted from

  • Devenish, S.R.; Huisman, F.H.; Parker, E.J.; Hadfield, A.T.; Gerrard, J.A.
    Cloning and characterisation of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis (2009), Biochim. Biophys. Acta, 1794, 1168-1174.
    View publication on PubMed
Search for more literature for 4.3.3.7

Application

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(Commentary)

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 (Commentary)

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

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 [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 [Da] Molecular Weight Maximum [Da] Comment Organism
31510
-
 mass spectrometry Neisseria meningitidis

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Neisseria meningitidis Q9JZR4
-
-
Neisseria meningitidis MC58 Q9JZR4
-
-

Purification (Commentary)

Purification (Comment) Organism
by centrifugation and gel filtration Escherichia coli
by centrifugation and gel filtration, to homogeneity Neisseria meningitidis

Substrates and Products (Substrate)

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

Subunits Comment Organism
homotetramer crystallography Neisseria meningitidis

Synonyms

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 [°C]

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 [1/s]

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 [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 IC50 Value Maximum Comment Organism Inhibitor Structure
0.053
-
-
 Neisseria meningitidis L-lysine

kcat/KM [mM/s]

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