Literature summary for 2.7.2.4 extracted from

Manjasetty, B.A.; Chance, M.R.; Burley, S.K.; Panjikar, S.; Almo, S.C.
Crystal structure of Clostridium acetobutylicum aspartate kinase (CaAK): an important allosteric enzyme for amino acids production (2014), Biotechnol. Rep., 3, 73-85.

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli TOP10 cells	Clostridium acetobutylicum

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified reombinant C-terminally His6-tagged enzyme, wild-type and SeMet-labelled proteins, hanging drop vapour diffusion method, mixing of 00013 ml rotein solution with 0.0013 m of reservoir solution containing 13% PEG 3350, and 100mM Tris HCl, pH 6.5, and equilibration against 0.5 ml of reservoir solution, microseeding, X-ray diffraction structure determination and analysis at 3.0 A resolution, modelling	Clostridium acetobutylicum

Crystallization (Comment)

Organism

purified reombinant C-terminally His6-tagged enzyme, wild-type and SeMet-labelled proteins, hanging drop vapour diffusion method, mixing of 00013 ml rotein solution with 0.0013 m of reservoir solution containing 13% PEG 3350, and 100mM Tris HCl, pH 6.5, and equilibration against 0.5 ml of reservoir solution, microseeding, X-ray diffraction structure determination and analysis at 3.0 A resolution, modelling

Clostridium acetobutylicum

Inhibitors

Inhibitors	Comment	Organism	Structure
L-lysine	threonine and lysine exhibit concerted feedback inhibition of asparatate kinase. Large conformational changes in the catalytic domain are associated with the lysine binding at the regulatory domains, L-lysine binding site structure, overview	Clostridium acetobutylicum
L-threonine	threonine and lysine exhibit concerted feedback inhibition of asparatate kinase	Clostridium acetobutylicum

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Clostridium acetobutylicum

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
48030	-	-	Clostridium acetobutylicum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-aspartate	Clostridium acetobutylicum	-	ADP + 4-phospho-L-aspartate	-	?

Organism

Organism	UniProt	Comment	Textmining
Clostridium acetobutylicum	Q97MC0	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant C-terminally His6-tagged enzyme from Escherichia coli TOP10 cells by nickel affinity chromatography and gel filtration	Clostridium acetobutylicum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-aspartate	-	Clostridium acetobutylicum	ADP + 4-phospho-L-aspartate	-	?
ATP + L-aspartate	transfer of the gamma-phosphate group of ATP to aspartate, substrate binding site structures, overview	Clostridium acetobutylicum	ADP + 4-phospho-L-aspartate	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme is composed of two domains: an N-terminal catalytic domain (kinase) domain and a C-terminal regulatory domain further comprised of two small domains belonging to the ACT domain family. Bending regions are in the vicinity of ATP binding site involved in domain movements between the catalytic and regulatory domains. Tetramer formation, overview	Clostridium acetobutylicum
tetramer	4 * 48030, dimer of dimers, sequence calculation and structure comparisons, three tetramers of CaAK comprise six homodimers which exhibits essentially identical overall dimeric architecture, T-state homodimeric architecture of CaAK, overview	Clostridium acetobutylicum

Cofactor

Cofactor	Comment	Organism	Structure
ATP	nucleotide binding structure, overview	Clostridium acetobutylicum

General Information

General Information	Comment	Organism
evolution	the enzyme is composed of two domains: an N-terminal catalytic domain (kinase) domain and a C-terminal regulatory domain further comprised of two small domains belonging to the ACT domain family. The enzyme CaAK monomer from Clostridium acetobutylicum belongs to the class I type aspartate kinases which consists of one catalytic domain and two ACT domains	Clostridium acetobutylicum
metabolism	the enzyme catalyzes the first step in the aspartate-derived amino acid pathway. Synthesis of 4-phospho-L-aspartate from L-aspartate is an intermediate step at an important branch point where one path leads to the synthesis of lysine and the other to threonine, methionine and isoleucine. The aspartate kinase enzymes exhibit complex allosteric regulation	Clostridium acetobutylicum
additional information	structure-function analysis, overview	Clostridium acetobutylicum
physiological function	the enzyme is tightly regulated through feedback control and responsible for the synthesis of 4-phospho-L-aspartate from L-aspartate. The aspartate kinase enzymes exhibit complex allosteric regulation	Clostridium acetobutylicum