Literature summary for 4.3.3.7 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.

Cloned(Commentary)

Cloned (Comment)	Organism
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

Cloned (Comment)

Organism

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)

Crystallization (Comment)	Organism
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

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

Purification (Commentary)

Purification (Comment)	Organism
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]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
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
1.5	-	purified enzyme, recombinant enzyme in the absence of the substrate pyruvate	Bacillus anthracis
2	-	crude extract, recombinant enzyme in the absence of the substrate pyruvate	Bacillus anthracis
12	-	crude extract, recombinant enzyme in the presence of the substrate pyruvate	Bacillus anthracis
33	-	purified enzyme, recombinant enzyme in the presence of the substrate pyruvate	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	-	?

Synonyms

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