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Literature summary extracted from

  • Griffin, M.D.; Dobson, R.C.; Gerrard, J.A.; Perugini, M.A.
    Exploring the dihydrodipicolinate synthase tetramer: how resilient is the dimer-dimer interface? (2010), Arch. Biochem. Biophys., 494, 58-63.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.3.7 DHDPS mutants expressed in Escherichia coli strain AT997r- Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.3.3.7 D193A removal of water mediated hydrogen-bond network Escherichia coli
4.3.3.7 D193Y removal of water mediated hydrogen-bond network and introduction of steric bulk to alter surface topology Escherichia coli
4.3.3.7 Q196D removal of hydrogen bonds and charge-charge repulsion, shortened side chain places charged carboxyl groups proximal at interface Escherichia coli
4.3.3.7 Q234D removal of hydrogen bond and charge-charge repulsion with negatively charged E175. Quaternary structure appears closest to that of the wild-type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.3.7 L-lysine
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.3.7 0.13
-
 L-aspartate 4-semialdehyde wild-type, at 30°C Escherichia coli
4.3.3.7 0.15
-
 L-aspartate 4-semialdehyde mutants Q196D, D193A and D193Y, at 30°C Escherichia coli
4.3.3.7 0.16
-
 pyruvate wild-type, at 30°C Escherichia coli
4.3.3.7 0.17
-
 L-aspartate 4-semialdehyde mutant D193A, at 30°C Escherichia coli
4.3.3.7 0.32
-
 pyruvate mutant Q196D, at 30°C Escherichia coli
4.3.3.7 0.44
-
 pyruvate mutant D193A, at 30°C Escherichia coli
4.3.3.7 0.46
-
 pyruvate mutant Q234D, at 30°C Escherichia coli
4.3.3.7 0.57
-
 pyruvate mutant D193Y, at 30°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.7 Escherichia coli P0A6L2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.3.7 wild-type DHDPS, and the coupling enzyme, DHDPR, by ammonium sulphate fractionation Escherichia coli

Storage Stability

EC Number Storage Stability Organism
4.3.3.7 -20°C, 20 mM Tris-HCl buffer, pH 8.0 Escherichia coli

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
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.3.7 tetramer the dimer-dimer interface is small, accounts only 4.3% of the subunit surface area Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.3.3.7 DapA
-
 Escherichia coli
4.3.3.7 DHDPS
-
 Escherichia coli
4.3.3.7 dihydrodipicolinate synthase
-
 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 6.5
-
 L-aspartate 4-semialdehyde mutant D193Y, at 30°C Escherichia coli
4.3.3.7 7.2
-
 pyruvate mutant D193Y, at 30°C Escherichia coli
4.3.3.7 9.15
-
 pyruvate mutant D193A, at 30°C Escherichia coli
4.3.3.7 11.8
-
 pyruvate mutant Q234D, at 30°C Escherichia coli
4.3.3.7 12.4
-
 L-aspartate 4-semialdehyde mutant D193A, at 30°C Escherichia coli
4.3.3.7 13.28
-
 pyruvate mutant Q196D, at 30°C Escherichia coli
4.3.3.7 78
-
 pyruvate wild-type, at 30°C Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.3.3.7 0.18
-
 L-lysine mutant D193A, with respect to (S)-aspartate 4-semialdehyde Escherichia coli
4.3.3.7 0.19
-
 L-lysine mutant Q196D, with respect to (S)-aspartate 4-semialdehyde Escherichia coli
4.3.3.7 0.4
-
 L-lysine wild-type, with respect to (S)-aspartate 4-semialdehyde Escherichia coli
4.3.3.7 2.2
-
 L-lysine mutant D193A, with respect to pyruvate Escherichia coli
4.3.3.7 3.6
-
 L-lysine wild-type, with respect to pyruvate Escherichia coli
4.3.3.7 4.1
-
 L-lysine mutant Q196D, with respect to pyruvate Escherichia coli

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 12.6
-
 pyruvate mutant D193Y, at 30°C Escherichia coli
4.3.3.7 21
-
 pyruvate mutant D193A, at 30°C Escherichia coli
4.3.3.7 25.6
-
 pyruvate mutant Q234D, at 30°C Escherichia coli
4.3.3.7 42
-
 pyruvate mutant Q196D, at 30°C Escherichia coli
4.3.3.7 43
-
 L-aspartate 4-semialdehyde mutant D193Y, at 30°C Escherichia coli
4.3.3.7 53
-
 L-aspartate 4-semialdehyde mutant D193A, at 30°C Escherichia coli
4.3.3.7 83
-
 L-aspartate 4-semialdehyde mutant D193A, at 30°C Escherichia coli
4.3.3.7 88
-
 L-aspartate 4-semialdehyde mutant Q196D, at 30°C Escherichia coli
4.3.3.7 488
-
 pyruvate wild-type, at 30°C Escherichia coli
4.3.3.7 600
-
 L-aspartate 4-semialdehyde wild-type, at 30°C Escherichia coli