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Literature summary extracted from

  • Hayashi, H.; Inoue, K.; Nagata, T.; Kuramitsu, S.; Kagamiyama, H.
    Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase (1993), Biochemistry, 32, 12229-12239.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.57 overexpression in Escherichia coli Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.57 additional information
-
 additional information Km values of half-reactions Escherichia coli
2.6.1.57 0.26
-
 L-phenylalanine pH 8.0, 25°C Escherichia coli
2.6.1.57 0.32
-
 L-tyrosine pH 8.0, 25°C, cosubstrate 2-oxoglutarate Escherichia coli
2.6.1.57 0.5
-
 L-tryptophan pH 8.0, 25°C, cosubstrate 2-oxoglutarate Escherichia coli
2.6.1.57 0.59
-
 2-oxoglutarate pH 8.0, 25°C, cosubstrate tryptophan Escherichia coli
2.6.1.57 0.8
-
 2-oxoglutarate pH 8.0, 25°C, cosubstrate aspartate Escherichia coli
2.6.1.57 1.3
-
 2-oxoglutarate pH 8.0, 25°C, cosubstrate tyrosine Escherichia coli
2.6.1.57 1.7
-
 2-oxoglutarate pH 8.0, 25°C, cosubstrate phenylalanine Escherichia coli
2.6.1.57 3.8
-
 L-aspartate pH 8.0, 25°C, cosubstrate 2-oxoglutarate Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.57 43000
-
 2 * 43000, SDS-PAGE Escherichia coli
2.6.1.57 43537
-
 2 * 43537, deduced from nucleotide sequence Escherichia coli
2.6.1.57 83000
-
 gel filtration Escherichia coli

Organism

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6.1.57 170
-
-
 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
-
 r
2.6.1.57 L-tyrosine + 2-oxoglutarate
-
 Escherichia coli p-hydroxyphenylpyruvate + L-glutamate
-
 r

Subunits

EC Number Subunits Comment Organism
2.6.1.57 dimer 2 * 43000, SDS-PAGE Escherichia coli
2.6.1.57 dimer 2 * 43537, deduced from nucleotide sequence Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.57 140
-
 L-aspartate pH 8.0, 25°C, cosubstrate 2-oxoglutarate Escherichia coli
2.6.1.57 160
-
 L-tryptophan pH 8.0, 25°C, cosubstrate 2-oxoglutarate Escherichia coli
2.6.1.57 210
-
 L-tyrosine pH 8.0, 25°C, cosubstrate 2-oxoglutarate Escherichia coli
2.6.1.57 250
-
 L-phenylalanine pH 8.0, 25°C, cosubstrate 2-oxoglutarate Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.57 pyridoxal 5'-phosphate a pyridoxal phosphate protein Escherichia coli