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Literature summary extracted from

  • Powell, J.T.; Morrison, J.F.
    The purification and properties of the aspartate aminotransferase and aromatic-amino-acid aminotransferase from Escherichia coli (1978), Eur. J. Biochem., 87, 391-400.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.6.1.57 inactivated by freezing Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.57 0.032
-
 4-hydroxyphenylpyruvate pH 7.6, 37°C Escherichia coli
2.6.1.57 0.042
-
 L-tyrosine pH 7.6, 37°C Escherichia coli
2.6.1.57 0.056
-
 phenylpyruvate pH 7.6, 37°C Escherichia coli
2.6.1.57 0.06
-
 L-phenylalanine pH 7.6, 37°C Escherichia coli
2.6.1.57 0.23
-
 2-oxoglutarate pH 7.6, 37°C Escherichia coli
2.6.1.57 0.28
-
 L-glutamate pH 7.6, 37°C Escherichia coli
2.6.1.57 0.5
-
 L-tryptophan pH 7.6, 37°C Escherichia coli
2.6.1.57 1.5
-
 L-methionine pH 7.6, 37°C Escherichia coli
2.6.1.57 2
-
 2-oxo-4-methylpentanoate pH 7.6, 37°C Escherichia coli
2.6.1.57 3.8
-
 oxaloacetate pH 7.6, 37°C Escherichia coli
2.6.1.57 5
-
 L-aspartate pH 7.6, 37°C Escherichia coli
2.6.1.57 5.8
-
 L-leucine pH 7.6, 37°C Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.57 46000
-
 2 * 46000, SDS-PAGE Escherichia coli
2.6.1.57 90000
-
 gel filtration Escherichia coli

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.57 ammonium sulfate, SAH-Sepharose, hydroxyapatite, pyridoxamine 5'-phosphate-Sepharose Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
2.6.1.57 an aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate ping-pong mechanism Escherichia coli
a

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-leucine + 2-oxoglutarate
-
 Escherichia coli 4-methyl-2-oxopentanoate + L-glutamate
-
 ?
2.6.1.57 L-methionine + 2-oxoglutarate
-
 Escherichia coli 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 ?
2.6.1.57 L-phenylalanine + 2-oxoglutarate
-
 Escherichia coli phenylpyruvate + L-glutamate
-
 r
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 i.e. 3-(4-hydroxyphenyl)-2-oxobutanoate + L-Glu r

Subunits

EC Number Subunits Comment Organism
2.6.1.57 dimer 2 * 46000, SDS-PAGE Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.57 7.2 7.6 phenylalanine Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.57 pyridoxal 5'-phosphate a pyridoxal phosphate protein Escherichia coli
2.6.1.57 pyridoxal 5'-phosphate apoenzyme can be reactivated with pyridoxal 5'-phosphate to a maximum of 60-70% activity in the presence of 2-oxoglutarate Escherichia coli