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Literature summary for 4.3.1.1 extracted from

  • Zhang, H.Y.; Zhang, J.; Lin, L.; Du, W.Y.; Lu, J.
    Enhancement of stability and activity of aspartase by random and site-directed mutagenesis (1993), Biochem. Biophys. Res. Commun., 192, 15-21.
    View publication on PubMed
Search for more literature for 4.3.1.1

Protein Variants

Protein Variants Comment Organism
K126R replacement of Lys126 with Arg increases the activity of the enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 AS 1.881 (wild-type)
-
Escherichia coli
-
 J2 (mutant of AS 1.881)
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate r Escherichia coli fumarate + NH3
-
 ?
L-aspartate natural substrate Escherichia coli fumarate + NH3
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
-
 Escherichia coli
50
-
 83% loss of activity (wild-type), 70% loss of activity (mutant enzyme) after 45 min Escherichia coli
60
-
 complete loss of activity after 5 min Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
-
 Escherichia coli
8
-
 wild-type enzyme, mutant enzyme (random mutagenesis) Escherichia coli
8.5
-
 mutant (site-directed) enzyme Escherichia coli

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 9 mutant enzyme by random mutagenesis Escherichia coli
7 9 mutant enzyme by site-directed mutagenesis Escherichia coli
7 8 wild-type enzyme Escherichia coli