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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.2.4 R169A site-directed mutagenesis, the Km for aspartate is decreased compared to the wild-type enzyme Corynebacterium pekinense
2.7.2.4 R169D site-directed mutagenesis, the mutant shows 2.57fold higher catalytic activity with aspartate than the wild-type enzyme Corynebacterium pekinense
2.7.2.4 R169H site-directed mutagenesis, the mutant shows 2.13fold higher catalytic activity with aspartate than the wild-type enzyme Corynebacterium pekinense
2.7.2.4 R169P site-directed mutagenesis, the mutant shows 2.25fold higher catalytic activity with aspartate than the wild-type enzyme Corynebacterium pekinense
2.7.2.4 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

EC Number Inhibitors Comment Organism Structure
2.7.2.4 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
2.7.2.4 L-methionine
-
 Corynebacterium pekinense
2.7.2.4 L-threonine
-
 Corynebacterium pekinense
2.7.2.4 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]

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.4 Mg2+ required Corynebacterium pekinense

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.2.4 18000
-
-
 Corynebacterium pekinense
2.7.2.4 47000
-
-
 Corynebacterium pekinense
2.7.2.4 130000
-
 native PAGE Corynebacterium pekinense

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 Corynebacterium pekinense
-
 ADP + 4-phospho-L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Corynebacterium pekinense E0AE72
-
-

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.7.2.4 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]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.2.4 26
-
 wild-type enzyme Corynebacterium pekinense
2.7.2.4 35
-
 mutant R169Y Corynebacterium pekinense

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.2.4 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.4 7
-
 wild-type enzyme Corynebacterium pekinense
2.7.2.4 9
-
 mutant R169Y Corynebacterium pekinense

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.7.2.4 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

EC Number Cofactor Comment Organism Structure
2.7.2.4 ATP
-
 Corynebacterium pekinense

General Information

EC Number General Information Comment Organism
2.7.2.4 evolution the enzyme from Corynebacterium pekinense belongs to the class II of aspartate kinases Corynebacterium pekinense
2.7.2.4 metabolism aspartate kinase is the key enzyme in the biosynthesis of aspartate derived amino acids Corynebacterium pekinense
2.7.2.4 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
2.7.2.4 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