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Literature summary for 2.7.2.4 extracted from

  • Wei, Z.; Han, C.; Gao, Y.; Fan, Z.; Wang, Y.; Wang, Z.; Min, W.
    Construction and enzymatic characterization of novel aspartokinase mutant Y198N/D201M from Corynebacterium pekinense (2020), Sh. Kexue/Food Sci., 41, 127-133 .
No PubMed abstract available
Search for more literature for 2.7.2.4

Protein Variants

Protein Variants Comment Organism
Y198N/D201M the mutant shows 18.26fold increased activity compared to the wild type enzyme, is less inhibited by L-lysine and L-threonine and activated by Lys + Met, Thr + Met, Lys + Thr + Met at 5 and 10 mM concentration Corynebacterium pekinense

Inhibitors

Inhibitors Comment Organism Structure
L-lysine
-
 Corynebacterium pekinense
L-threonine
-
 Corynebacterium pekinense

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.37
-
 L-aspartate mutant enzyme Y198N/D201M, at pH 7.5 and 25°C Corynebacterium pekinense
3.58
-
 L-aspartate wild type enzyme, at pH 7.5 and 25°C 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
-
-
-

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
-
 Corynebacterium pekinense

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
 the wild type enzyme has a half-life of 4.66 h at 25°C Corynebacterium pekinense

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Corynebacterium pekinense