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Literature summary for 4.3.1.1 extracted from

  • Wang, L.J.; Kong, X.D.; Zhang, H.Y.; Wang, X.P.; Zhang, J.
    Enhancement of the activity of l-aspartase from Escherichia coli W by directed evolution (2000), Biochem. Biophys. Res. Commun., 276, 346-349.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information mutant N217K/T233R/V367G through enzyme modification by direct evolution in order to enhance enzymic activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2
-
L-aspartate wild type Escherichia coli
2.6
-
L-aspartate mutant N217K/T233R/V367G Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
wild type Escherichia coli
8.2
-
mutant N217K/T233R/V367G Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7 8 mutant N217K/T233R/V367G Escherichia coli
7.8 9.3 evolved enzyme Escherichia coli