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Literature summary 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

Application

EC Number Application Comment Organism
4.3.3.7 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)

EC Number Cloned (Comment) Organism
4.3.3.7 as His-tagged constructs Escherichia coli
4.3.3.7 into the expression vector pET151-D to give the plasmid pFH02, to transform chemically super-competent Escherichia coli Top10 cells Neisseria meningitidis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.3.7 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

EC Number Inhibitors Comment Organism Structure
4.3.3.7 L-aspartate 4-semialdehyde is subject to substrate inhibition by high concentrations Neisseria meningitidis
4.3.3.7 L-lysine
-
 Escherichia coli
4.3.3.7 L-lysine is significantly more sensitive to feedback inhibition than Escherichia coli DHDPS Neisseria meningitidis
4.3.3.7 additional information no substrate inhibition by (S)-aspartate 4-semialdehyde Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.3.7 0.052
-
 L-aspartate 4-semialdehyde at 30°C, in 100 mM HEPES buffer, pH 8.0 Neisseria meningitidis
4.3.3.7 0.11
-
 L-aspartate 4-semialdehyde at 30°C, in 100 mM HEPES buffer, pH 8.0 Escherichia coli
4.3.3.7 0.26
-
 pyruvate at 30°C, in 100 mM HEPES buffer, pH 8.0 Escherichia coli
4.3.3.7 0.5
-
 pyruvate at 30°C, in 100 mM HEPES buffer, pH 8.0 Neisseria meningitidis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.3.7 31510
-
 mass spectrometry Neisseria meningitidis

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.7 Escherichia coli
-
-
-
4.3.3.7 Neisseria meningitidis Q9JZR4
-
-
4.3.3.7 Neisseria meningitidis MC58 Q9JZR4
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.3.7 L-aspartate 4-semialdehyde + pyruvate
-
 Escherichia coli dihydrodipicolinate + 2 H2O
-
 ?
4.3.3.7 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
-
 ?
4.3.3.7 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

EC Number Subunits Comment Organism
4.3.3.7 homotetramer crystallography Neisseria meningitidis

Synonyms

EC Number Synonyms Comment Organism
4.3.3.7 DapA
-
 Escherichia coli
4.3.3.7 DapA
-
 Neisseria meningitidis
4.3.3.7 DHDPS
-
 Escherichia coli
4.3.3.7 DHDPS
-
 Neisseria meningitidis
4.3.3.7 dihydrodipicolinate synthase
-
 Escherichia coli
4.3.3.7 dihydrodipicolinate synthase
-
 Neisseria meningitidis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.3.3.7 46.5
-
 melting temperature in the absence of substrates Neisseria meningitidis
4.3.3.7 59.5
-
 melting temperature in the absence of substrates Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.3.7 46.7
-
 pyruvate at 30°C, in 100 mM HEPES buffer, pH 8.0 Neisseria meningitidis
4.3.3.7 124
-
 pyruvate at 30°C, in 100 mM HEPES buffer, pH 8.0 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.3.3.7 0.058
-
 L-lysine with (S)-aspartate 4-semialdehyde as substrate Neisseria meningitidis
4.3.3.7 0.32
-
 L-lysine with (S)-aspartate 4-semialdehyde as substrate Escherichia coli
4.3.3.7 1.7
-
 L-lysine with pyruvate as substrate Neisseria meningitidis
4.3.3.7 3.9
-
 L-lysine with pyruvate as substrate Escherichia coli

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
4.3.3.7 0.053
-
-
 Neisseria meningitidis L-lysine

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.3.3.7 93.4
-
 pyruvate at 30°C, in 100 mM HEPES buffer, pH 8.0 Neisseria meningitidis
4.3.3.7 898
-
 L-aspartate 4-semialdehyde at 30°C, in 100 mM HEPES buffer, pH 8.0 Neisseria meningitidis