Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Hayashi, H.; Inoue, K.; Mizuguchi, H.; Kagamiyama, H.
    Analysis of the substrate-recognition mode of aromatic amino acid aminotransferase by combined use of quasisubstrates and site-directed mutagenesis: systematic hydroxy-group addition/deletion studies to probe the enzyme-substrate interactions (1996), Biochemistry, 35, 6754-6761.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.6.1.57 R292A very low activity with aspartate, 5-10fold increase in Km for aromatic amino acids Escherichia coli
2.6.1.57 R292K very low activity with aspartate, 10-100fold increase in Km for aromatic amino acids Escherichia coli
2.6.1.57 R292L very low activity with aspartate, 5-10fold increase in Km for aromatic amino acids Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.57 0.68
-
L-tryptophan pH 8.0, 25°C, single-turnover, wild-type enzyme Escherichia coli
2.6.1.57 0.83
-
L-tyrosine pH 8.0, 25°C, single-turnover, wild-type enzyme Escherichia coli
2.6.1.57 1
-
L-phenylalanine pH 8.0, 25°C, single-turnover, wild-type enzyme Escherichia coli
2.6.1.57 5
-
L-aspartate pH 8.0, 25°C, single-turnover, wild-type enzyme Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.57 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.57 aspartate + 2-oxoglutarate
-
Escherichia coli oxaloacetate + L-glutamate
-
r
2.6.1.57 L-phenylalanine + 2-oxoglutarate
-
Escherichia coli phenylpyruvate + L-glutamate
-
?
2.6.1.57 L-tryptophan + 2-oxoglutarate
-
Escherichia coli 3-indole-2-oxopropanoate + L-glutamate
-
?
2.6.1.57 L-tyrosine + 2-oxoglutarate
-
Escherichia coli p-hydroxyphenylpyruvate + L-glutamate
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.57 290
-
L-aspartate pH 8.0, 25°C, single-turnover, wild-type enzyme Escherichia coli
2.6.1.57 350
-
L-tryptophan pH 8.0, 25°C, single-turnover, wild-type enzyme Escherichia coli
2.6.1.57 500
-
L-tyrosine pH 8.0, 25°C, single-turnover, wild-type enzyme Escherichia coli
2.6.1.57 1200
-
L-phenylalanine pH 8.0, 25°C, single-turnover, wild-type enzyme Escherichia coli