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Literature summary for 2.6.1.57 extracted from

  • Mavrides, C.; Orr, W.
    Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli (1975), J. Biol. Chem., 250, 4128-4133.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.33
-
L-phenylalanine
-
Escherichia coli
0.62
-
L-tyrosine
-
Escherichia coli
2.5
-
2-oxoglutarate
-
Escherichia coli
3.13
-
oxaloacetate
-
Escherichia coli
10
-
L-tryptophan
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
88000
-
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 42000-45000, SDS-PAGE Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
10 min, less than 10% of original activity towards tyrosine and phenylalanine Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
tryptophan Escherichia coli
8
-
with tyrosine Escherichia coli
8
-
with phenylalanine Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6 9.5 approx. 45% of maximal activity at pH 6.0,: approx. 60% of maximal activity at pH 9.5, phenylalanine Escherichia coli
6 10 approx. 40% of maximal activity at pH 6.0, tryptophan Escherichia coli
6 10 approx. 25% of maximal activity at pH 10.0, tryptophan Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate Km: 0.01 mM Escherichia coli
pyridoxal 5'-phosphate a pyridoxal phosphate protein Escherichia coli