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Literature summary for 4.3.3.7 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
Search for more literature for 4.3.3.7

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
D193A removal of water mediated hydrogen-bond network Escherichia coli
D193Y removal of water mediated hydrogen-bond network and introduction of steric bulk to alter surface topology Escherichia coli
Q196D removal of hydrogen bonds and charge-charge repulsion, shortened side chain places charged carboxyl groups proximal at interface Escherichia coli
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

Inhibitors Comment Organism Structure
L-lysine
-
 Escherichia coli

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6L2
-
-

Purification (Commentary)

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

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
DapA
-
 Escherichia coli
DHDPS
-
 Escherichia coli
dihydrodipicolinate synthase
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.5
-
 L-aspartate 4-semialdehyde mutant D193Y, at 30°C Escherichia coli
7.2
-
 pyruvate mutant D193Y, at 30°C Escherichia coli
9.15
-
 pyruvate mutant D193A, at 30°C Escherichia coli
11.8
-
 pyruvate mutant Q234D, at 30°C Escherichia coli
12.4
-
 L-aspartate 4-semialdehyde mutant D193A, at 30°C Escherichia coli
13.28
-
 pyruvate mutant Q196D, at 30°C Escherichia coli
78
-
 pyruvate wild-type, at 30°C Escherichia coli

Ki Value [mM]

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

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
12.6
-
 pyruvate mutant D193Y, at 30°C Escherichia coli
21
-
 pyruvate mutant D193A, at 30°C Escherichia coli
25.6
-
 pyruvate mutant Q234D, at 30°C Escherichia coli
42
-
 pyruvate mutant Q196D, at 30°C Escherichia coli
43
-
 L-aspartate 4-semialdehyde mutant D193Y, at 30°C Escherichia coli
53
-
 L-aspartate 4-semialdehyde mutant D193A, at 30°C Escherichia coli
83
-
 L-aspartate 4-semialdehyde mutant D193A, at 30°C Escherichia coli
88
-
 L-aspartate 4-semialdehyde mutant Q196D, at 30°C Escherichia coli
488
-
 pyruvate wild-type, at 30°C Escherichia coli
600
-
 L-aspartate 4-semialdehyde wild-type, at 30°C Escherichia coli