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Literature summary extracted from

  • Voss, J.E.; Scally, S.W.; Taylor, N.L.; Dogovski, C.; Alderton, M.R.; Hutton, C.A.; Gerrard, J.A.; Parker, M.W.; Dobson, R.C.; Perugini, M.A.
    Expression, purification, crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase from Bacillus anthracis in the presence of pyruvate (2009), Acta Crystallogr. Sect. F, 65, 188-191.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.3.7 PCR product ligated into pCRBluntII-TOPO and transformed into Escherichia coli One Shot TOP10. The dapA insert then amplified, the product, which now contains NdeI and BamHI restriction-endonuclease sites, ligated into pCR-BluntII-TOPO and transformed into Escherichia coli One Shot TOP10, which enables efficient ligation into an expression vector. DapA and linearized pET-11a ligated with T4 DNA ligase and transformed into Escherichia coli BL21(DE3) Bacillus anthracis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.3.7 in the presence of pyruvate, the hanging-drop vapour-diffusion method, at a resolution of 2.15 A. Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 84.5, b = 124.6, c = 131.0 A, beta = 90.0 Bacillus anthracis

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.7 Bacillus anthracis Q81WN7 Sterne strain
-
4.3.3.7 Bacillus anthracis Sterne Q81WN7 Sterne strain
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.3.7 by gel filtration, recombinant enzyme in the absence of the substrate pyruvate (with a yield of 36.3%) and presence of the substrate pyruvate (with a yield of 98%) Bacillus anthracis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.3.7 additional information
-
 DHDPS purified in the presence of pyruvate yields a greater amount of recombinant enzyme with 22fold greater specific activity compared with the enzyme purified in the absence of substrate Bacillus anthracis
4.3.3.7 1.5
-
 purified enzyme, recombinant enzyme in the absence of the substrate pyruvate Bacillus anthracis
4.3.3.7 2
-
 crude extract, recombinant enzyme in the absence of the substrate pyruvate Bacillus anthracis
4.3.3.7 12
-
 crude extract, recombinant enzyme in the presence of the substrate pyruvate Bacillus anthracis
4.3.3.7 33
-
 purified enzyme, recombinant enzyme in the presence of the substrate pyruvate Bacillus anthracis

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
4.3.3.7 DapA
-
 Bacillus anthracis
4.3.3.7 DHDPS
-
 Bacillus anthracis
4.3.3.7 dihydrodipicolinate synthase
-
 Bacillus anthracis