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Literature summary for 2.6.1.1 extracted from

  • Wang, N.C.; Lee, C.Y.
    Enhanced transaminase activity of a bifunctional L-aspartate 4-decarboxylase (2007), Biochem. Biophys. Res. Commun., 356, 368-373.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
Y225R/R292K/R386A the mutation converts its activity into an aspartate 4-decarboxylase Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P00509
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.06
-
wild type enzyme, at 37°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
Escherichia coli oxaloacetate + L-glutamate
-
?

Synonyms

Synonyms Comment Organism
AspAT
-
Escherichia coli