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Literature summary for 4.3.3.7 extracted from

  • Voss, J.E.; Scally, S.W.; Taylor, N.L.; Atkinson, S.C.; Griffin, M.D.; Hutton, C.A.; Parker, M.W.; Alderton, M.R.; Gerrard, J.A.; Dobson, R.C.; Dogovski, C.; Perugini, M.A.
    Substrate-mediated stabilization of a tetrameric drug target reveals Achilles heel in anthrax (2010), J. Biol. Chem., 285, 5188-5195.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.3.3.7

Cloned(Commentary)

Cloned (Comment) Organism
dapA gene encoding DHDPS amplified and cloned into the pET11a expression vector, expressed in Escherichia coli BL21-DE3 Bacillus anthracis

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with pyruvate, by sitting- and hanging-drop vapor diffusion method, to 2.15 A resolution, shares the same space group, unit cell parameters, and a similar resolution to the structure of substrate unbound DHDPS. Twelve more hydrogen bond interactions at both interfaces in the crystal structure of pyruvate-bound DHDPS relative to the apo structure Bacillus anthracis

Protein Variants

Protein Variants Comment Organism
L170E/G191E dimeric mutant of the enzyme, retains only 1.8% of the total catalytic activity of the wild-type tetrameric enzyme Bacillus anthracis

General Stability

General Stability Organism
the secondary and quaternary structure is significantly stabilized in the presence of pyruvate Bacillus anthracis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
 L-aspartate 4-semialdehyde mutant L170E/G191E, at 30°C Bacillus anthracis
0.25
-
 L-aspartate 4-semialdehyde wild-type, at 30°C Bacillus anthracis
1.2
-
 pyruvate wild-type, at 30°C Bacillus anthracis
3.7
-
 pyruvate mutant L170E/G191E, at 30°C Bacillus anthracis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31000
-
 2 * 31000, calculated from sequence Bacillus anthracis
31000
-
 4 * 31000, calculated from sequence Bacillus anthracis
124000
-
 wild-type, sequence analysis Bacillus anthracis

Organism

Organism UniProt Comment Textmining
Bacillus anthracis Q81WN7 Sterne strain
-
Bacillus anthracis Sterne Q81WN7 Sterne strain
-

Purification (Commentary)

Purification (Comment) Organism
by sonication, anion-exchange and hydrophobic interaction liquid chromatography Bacillus anthracis

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 31000, calculated from sequence Bacillus anthracis
More the tetramer-dimer dissociation constant of the enzyme is 3fold tighter in the presence of pyruvate compared with the apo form Bacillus anthracis
tetramer 4 * 31000, calculated from sequence Bacillus anthracis

Synonyms

Synonyms Comment Organism
DHDPS
-
 Bacillus anthracis
dihydrodipicolinate synthase
-
 Bacillus anthracis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50 60 thermostability is significantly enhanced in the presence of the substrate pyruvate Bacillus anthracis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.7
-
 pyruvate mutant L170E/G191E, at 30°C Bacillus anthracis
92
-
 pyruvate wild-type, at 30°C Bacillus anthracis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.46
-
 pyruvate mutant L170E/G191E, at 30°C Bacillus anthracis
34
-
 L-aspartate 4-semialdehyde mutant L170E/G191E, at 30°C Bacillus anthracis
76.67
-
 pyruvate wild-type, at 30°C Bacillus anthracis
368
-
 L-aspartate 4-semialdehyde wild-type, at 30°C Bacillus anthracis