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Literature summary 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.1 0.00025
-
 pyridoxyl 5'-phosphate pH 7.6, 25°C Escherichia coli
2.6.1.1 0.071
-
 2-oxoglutarate pH 7.6, 25°C Escherichia coli
2.6.1.1 0.37
-
 oxaloacetate pH 7.6, 25°C Escherichia coli
2.6.1.1 1.43
-
 L-tyrosine pH 7.6, 25°C Escherichia coli
2.6.1.1 2.17
-
 L-phenylalanine
-
 Escherichia coli
2.6.1.1 4.4
-
 L-aspartate
-
 Escherichia coli
2.6.1.1 5
-
 L-tryptophan pH 7.6, 25°C Escherichia coli
2.6.1.57 0.33
-
 L-phenylalanine
-
 Escherichia coli
2.6.1.57 0.62
-
 L-tyrosine
-
 Escherichia coli
2.6.1.57 2.5
-
 2-oxoglutarate
-
 Escherichia coli
2.6.1.57 3.13
-
 oxaloacetate
-
 Escherichia coli
2.6.1.57 10
-
 L-tryptophan
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.1 82000
-
 PAGE Escherichia coli
2.6.1.57 88000
-
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.1 L-aspartate + 2-oxoglutarate Escherichia coli
-
 oxaloacetate + L-glutamate
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.1
-
 Escherichia coli
2.6.1.57
-
 Escherichia coli

Storage Stability

EC Number Storage Stability Organism
2.6.1.1 4°C, stable for several weeks Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.1 L-aspartate + 2-oxoglutarate
-
 Escherichia coli oxaloacetate + L-glutamate
-
 ?
2.6.1.1 L-aspartate + 2-oxoglutarate
-
 Escherichia coli oxaloacetate + L-glutamate
-
 r
2.6.1.1 L-phenylalanine + 2-oxoglutarate
-
 Escherichia coli 2-oxo-3-phenylpropionic acid + L-glutamate i.e. phenylpyruvate ?
2.6.1.1 L-tryptophan + 2-oxoglutarate
-
 Escherichia coli 3-indole-2-oxopropionic acid + L-glutamate
-
 ?
2.6.1.1 L-tyrosine + 2-oxoglutarate
-
 Escherichia coli 3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate i.e. 4-hydroxyphenylpyruvate ?
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
2.6.1.1 dimer 2 * 42000-45000, SDS-PAGE Escherichia coli
2.6.1.57 dimer 2 * 42000-45000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.6.1.1 More EC 2.6.1.57 may be converted to EC 2.6.1.1 by controlled proteolysis with subtilisin, the 2 enzymes are encoded by 2 different genes with high sequence homology Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.57 37
-
 assay at Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.6.1.1 55
-
 10 min, 48% loss of activity with tyrosine, 36% loss of activity with phenylalanine Escherichia coli
2.6.1.57 55
-
 10 min, less than 10% of original activity towards tyrosine and phenylalanine Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.1 8
-
 formation of aspartate Escherichia coli
2.6.1.1 8.5
-
 substrates L-phenylalanine or L-tryptophan Escherichia coli
2.6.1.1 9
-
 substrate L-tyrosine Escherichia coli
2.6.1.57 7.5
-
 tryptophan Escherichia coli
2.6.1.57 8
-
 with tyrosine Escherichia coli
2.6.1.57 8
-
 with phenylalanine Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.6.1.57 6 9.5 approx. 45% of maximal activity at pH 6.0,: approx. 60% of maximal activity at pH 9.5, phenylalanine Escherichia coli
2.6.1.57 6 10 approx. 40% of maximal activity at pH 6.0, tryptophan Escherichia coli
2.6.1.57 6 10 approx. 25% of maximal activity at pH 10.0, tryptophan Escherichia coli

Cofactor

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