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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.2.4 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

EC Number Inhibitors Comment Organism Structure
2.7.2.4 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
2.7.2.4 L-threonine threonine and lysine exhibit concerted feedback inhibition of asparatate kinase Clostridium acetobutylicum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.4 Mg2+ required Clostridium acetobutylicum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.2.4 48030
-
-
 Clostridium acetobutylicum

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Clostridium acetobutylicum Q97MC0
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.4 ATP + L-aspartate
-
 Clostridium acetobutylicum ADP + 4-phospho-L-aspartate
-
 ?
2.7.2.4 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

EC Number Subunits Comment Organism
2.7.2.4 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
2.7.2.4 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

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

General Information

EC Number General Information Comment Organism
2.7.2.4 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
2.7.2.4 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
2.7.2.4 additional information structure-function analysis, overview Clostridium acetobutylicum
2.7.2.4 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