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Literature summary extracted from

  • Liu, X.; Pavlovsky, A.G.; Viola, R.E.
    The structural basis for allosteric inhibition of a threonine-sensitive aspartokinase (2008), J. Biol. Chem., 283, 16216-16225.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.7.2.4 additional information The absence of the aspartate biosynthetic pathway in humans makes it a good target for new pesticides and antibiotics. Methanocaldococcus jannaschii

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.2.4 pET-41a vector and Rosetta (DE3) Escherichia coli cells for protein expression Methanocaldococcus jannaschii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.2.4 3C20, 14% PEG4000, 0.1 M Tris, 0.8 M ammonium formate, pH 8.0, vapor diffusion, hanging drop, temperature 293 K, space group C2221, 3C1N, 0.2 M ammonium iodide, 2.2 M ammonium sulfate, pH 5.0, vapor diffusion, hanging drop, temperature 293 K, space group P212121, 3C1M, 14% PEG4000, 100 mM Tris, 800 mM ammonium formate, pH 8.0, vapor diffusion, hanging drop, temperature 293 K, space group P212121, the structure is determined under three different transition states: ternary complex with MgAMP-PNP and L-aspartate, binary complex with L-aspartate, and binary complex in the presence of its allosteric inhibitor L-threonine Methanocaldococcus jannaschii

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.4 L-threonine mechanism for allosteric regulation in which the domain movements induced by L-threonine binding causes displacement of the substrates from the enzyme, resulting in a relaxed, inactive conformation Methanocaldococcus jannaschii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.4 Mg2+
-
 Methanocaldococcus jannaschii

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 Methanocaldococcus jannaschii L-aspartate binds to this recombinant enzyme in two different orientations ADP + 4-phospho-L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Methanocaldococcus jannaschii Q57991 Methanococcus jannaschii has only a single, monofunctional form of AK; pET-41a vector and Rosetta (DE3) Escherichia coli cells for protein expression
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.2.4 two successive chromatography steps: first a high resolution anionic exchange resin, followed by gel filtration column, the resulting protein is shown by SDS-PAGE to be more than 99% pure, concentration to 30 mg/ml by using a 10000 molecular weight cut-off Amicon concentrator Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.4 ATP + L-aspartate L-aspartate binds to this recombinant enzyme in two different orientations Methanocaldococcus jannaschii ADP + 4-phospho-L-aspartate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.2.4 tetramer dimer of dimers Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
2.7.2.4 aspartokinase
-
 Methanocaldococcus jannaschii