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Literature summary for 2.6.1.57 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
Search for more literature for 2.6.1.57

General Stability

General Stability Organism
inactivated by freezing Escherichia coli

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

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

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
aspartate + 2-oxoglutarate
-
 Escherichia coli oxaloacetate + L-glutamate
-
 r
L-leucine + 2-oxoglutarate
-
 Escherichia coli 4-methyl-2-oxopentanoate + L-glutamate
-
 ?
L-methionine + 2-oxoglutarate
-
 Escherichia coli 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 ?
L-phenylalanine + 2-oxoglutarate
-
 Escherichia coli phenylpyruvate + L-glutamate
-
 r
L-tryptophan + 2-oxoglutarate
-
 Escherichia coli 3-indole-2-oxopropanoate + L-glutamate
-
 r
L-tyrosine + 2-oxoglutarate
-
 Escherichia coli p-hydroxyphenylpyruvate + L-glutamate i.e. 3-(4-hydroxyphenyl)-2-oxobutanoate + L-Glu r

Subunits

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2 7.6 phenylalanine Escherichia coli

Cofactor

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