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2.7.2.4: aspartate kinase

This is an abbreviated version!
For detailed information about aspartate kinase, go to the full flat file.

Word Map on EC 2.7.2.4

Reaction

ATP
+
L-aspartate
=
ADP
+
4-phospho-L-aspartate

Synonyms

AK, AK II, AK III, AK-HSDH, AK-HSDH I, AK-HSDH1, AK-HSDH2, AK-HseDH, AK-R7, AK-ts31d, AK1, AK2, AK3, AKbeta, AKII, AKIII, AKsyn, Ask, ASK1, ASK2, Ask_Ect, Ask_LysC, Asp kinase-homoserine dehydrogenase, aspartate kinase, aspartate kinase (phosphorylating), aspartate kinase 1, aspartate kinase 2, aspartate kinase 3, aspartate kinase beta, aspartate kinase I, aspartate kinase II, aspartate kinase III, aspartic kinase, aspartokinase, aspartokinase 1-homoserine dehydrogenase 1, aspartokinase 2, aspartokinase 3, aspartokinase I, aspartokinase II, aspartokinase III, aspartokinase-homoserine dehydrogenase, beta-aspartokinase, bifunctional aspartate kinase-homoserine dehydrogenase, BT, BTT, CgAK, dap-aspartokinase, HOM3 product, HOM3-R7 product, HOM3-ts31d product, HseDH, LT-aspartokinase, lysC, lysine-sensitive aspartokinase 3, More, MtbAKbeta, nspJ, Thr-sensitive aspartate kinase, thrA, thrA1, thrA2, TM_0547, XbAK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.2 Phosphotransferases with a carboxy group as acceptor
                2.7.2.4 aspartate kinase

Crystallization

Crystallization on EC 2.7.2.4 - aspartate kinase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
by the hanging-drop vapor-diffusion method, crystal structure of the regulatory subunit of AK at 1.58 A resolution in the Thr-binding form, regulatory subunit contains two ACT domain motifs per monomer and is arranged as a dimer, regulatory subunit is a monomer in the absence of Thr but becomes a dimer by adding Thr
the structure of the regulatory subiunit AKbeta complexed with threonine is determined at 1.58 A resolution, 0.2 M ammonium sulfate, 0.1 M citrate, 36%(w/v) PEG 4000, 10 mM threonine, pH 5.0, vapor diffusion, hanging drop, temperature 293 K, space group C 2 (C 1 2 1)
crystal structures analysis, overview
by sitting drop vapor-diffusion method, AKIII in the inactive T-state with bound feedback allosteric inhibitor L-lysine, to 2.8 A resolution, and in the R-state with L-aspartate and ADP, to 2.5 A resolution, unusual configuration for the regulatory ACT domains, in which ACT2 is inserted into ACT1 rather than the expected tandem repeat
-
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
by hanging-drop vapor-diffusion method, in the presence of L-aspartate and MgADP, to 2.82–2.69 A resolution, N-terminal catalytic domain (residues 2-300) and a C-terminal regulatory domain (residues 310-470) joined through a hinge region (residues 301-309)
crystal structure of the regulatory subunit of aspartate kinase from Mtb alone and in complex with threonine are determined at resolutions of 2.6 A and 2.0 A, respectively. MtbAKbeta is composed of two perpendicular non-equivalent ACT domains (aspartate kinase, chorismate mutase, and TyrA (prephenate dehydrogenase)) per monomer. Each ACT domain contains two alpha helices and four antiparallel beta strands
regulatory domain (AK-beta) in the presence of the potential feedback inhibitor threonine is crystallized to 1.6 A resolution. Crystal form belongs to space group P2-1-2-12-1, with unit-cell parameters a = 53.70, b = 63.43, c = 108.85 A and two molecules per asymmetric unit
-
hanging drop vapor diffusion method, using 0.4 M ammonium sulfate, 0.1 M sodium citrate tribasic dihydrate (pH 5.6) and 0.9 M lithium sulfate monohydrate
refined at 2.55 A resolution in complex with L-lysine and L-threonine
by hanging-drop vapour-diffusion method, regulatory subunit in the presence of the inhibitor threonine, to 2.15 A resolution, crystal belongs to the cubic space group P4332 or P4132, with unit-cell parameters a = b = c = 141.8 A
by the hanging-drop vapour-diffusion method using Crystal Screen kits, the regulatory subunit (the beta subunit of Thermus thermophilus AK) is crystallized in the presence of the inhibitor threonine. Diffraction data are collected to 2.15 A at a synchrotron source. The crystal belongs to the cubic space group P4332 or P4132, with unit-cell parameters a = b = c = 141.8 A.
enzyme free or in complex with L-threonine, hanging drop vapor diffusion method, using 0.1 M sodium acetate (pH 5.0) and 1.2-2.0 M NaCl