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Literature summary for 2.7.2.4 extracted from

  • Min, W.; Li, H.; Li, H.; Liu, C.; Liu, J.
    Characterization of Aspartate Kinase from Corynebacterium pekinense and the Critical Site of Arg169 (2015), Int. J. Mol. Sci., 16, 28270-28284.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.2.4

Cloned(Commentary)

Cloned (Comment) Organism
sequence comparisons, recombinant expression of wild-type and mutant enzymes Corynebacterium pekinense

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures analysis, overview Corynebacterium pekinense

Protein Variants

Protein Variants Comment Organism
R169A site-directed mutagenesis, the Km for aspartate is decreased compared to the wild-type enzyme Corynebacterium pekinense
R169D site-directed mutagenesis, the mutant shows 2.57fold higher catalytic activity with aspartate than the wild-type enzyme Corynebacterium pekinense
R169H site-directed mutagenesis, the mutant shows 2.13fold higher catalytic activity with aspartate than the wild-type enzyme Corynebacterium pekinense
R169P site-directed mutagenesis, the mutant shows 2.25fold higher catalytic activity with aspartate than the wild-type enzyme Corynebacterium pekinense
R169Y site-directed mutagenesis, the mutant shows 4.7fold higher catalytic activity with aspartate than the wild-type enzyme. The three-dimensional structure of R169Y is more stable than that of the wild-type Corynebacterium pekinense

Inhibitors

Inhibitors Comment Organism Structure
L-lysine each dimer contains two lysine binding sites, in which one site is exclusively found in the dimer with A and B chains located at the interface between alpha and beta subunits Corynebacterium pekinense
L-methionine
-
 Corynebacterium pekinense
L-threonine
-
 Corynebacterium pekinense
additional information aspartate kinase is an allosteric enzyme, and its activity is inhibited by allosteric inhibitors, such as Lys, Met, and Thr Corynebacterium pekinense

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics analysis of wild-type and mutant enzymes, overview Corynebacterium pekinense

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Corynebacterium pekinense

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
18000
-
-
 Corynebacterium pekinense
47000
-
-
 Corynebacterium pekinense
130000
-
 native PAGE Corynebacterium pekinense

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Corynebacterium pekinense E0AE72
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate
-
 Corynebacterium pekinense ADP + 4-phospho-L-aspartate
-
 ?

Subunits

Subunits Comment Organism
heterotetramer dimer of dimers, alpha2beta2-type structure, 2 * 47000, alpha-subunit + 2 * 18000, beta-subunit, SDS-PAGE, each dimer contains two lysine binding sites, in which one site is exclusively found in the dimer with A and B chains located at the interface between alpha and beta subunits Corynebacterium pekinense

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
26
-
 wild-type enzyme Corynebacterium pekinense
35
-
 mutant R169Y Corynebacterium pekinense

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
26
-
 purified recombinant proteins, pH 8.0, half-life of the wild-type enzyme is 4.5 h, and the half-life of the mutant R169Y increases to 5.5 h Corynebacterium pekinense

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 wild-type enzyme Corynebacterium pekinense
9
-
 mutant R169Y Corynebacterium pekinense

pH Stability

pH Stability pH Stability Maximum Comment Organism
8
-
 purified recombinant proteins, 26°C, half-life of the wild-type enzyme is 4.5 h, and the half-life of the mutant R169Y increases to 5.5 h Corynebacterium pekinense

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Corynebacterium pekinense

General Information

General Information Comment Organism
evolution the enzyme from Corynebacterium pekinense belongs to the class II of aspartate kinases Corynebacterium pekinense
metabolism aspartate kinase is the key enzyme in the biosynthesis of aspartate derived amino acids Corynebacterium pekinense
additional information catalytic residue Arg169 is an important residue in substrate binding, the catalytic domain, and in inhibitor binding. Arg169 forms a hydrogen bond with Glu92, which functions as the entrance gate. R169, S172, and G171 are key substrate binding residues. Three-dimensional structure analysis and structure homology modelling, overview Corynebacterium pekinense
physiological function aspartate kinase is a multimer and an allosteric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl phosphate. Allosteric regulation (feedback inhibition) of proteins controls the synthesis pathway of this enzyme Corynebacterium pekinense