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Literature summary for 2.6.1.1 extracted from

  • Yagi, T.; Kagamiyama, H.; Motosugi, K.; Nozaki, M.; Soda, K.
    Crystallization and properties of aspartate aminotransferase from Escherichia coli B (1979), FEBS Lett., 100, 81-84.
    View publication on PubMed
Search for more literature for 2.6.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
vapour diffusion technique, protein solution: 10 mg/ml, 10 mM potassium phosphate,pH 7.0, 2.5 mM pyridoxal 5'-phosphate, 2.5% polyethylene glycol w/v, 4°C, 7-10 days Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
 2 * 43000, SDS-PAGE Escherichia coli
80000 84000 gel filtration, meniscus depletion sedimentation equilibrium method Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate + 2-oxoglutarate Escherichia coli
-
 oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate Escherichia coli B / ATCC 11303
-
 oxaloacetate + L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 B
-
Escherichia coli B / ATCC 11303
-
 B
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Escherichia coli
210
-
 purified apoenzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
 Escherichia coli oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate 30% of the activity with glutamate Escherichia coli oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate
-
 Escherichia coli B / ATCC 11303 oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate 30% of the activity with glutamate Escherichia coli B / ATCC 11303 oxaloacetate + L-glutamate
-
 ?
L-glutamate + 2-oxoglutarate L-glutamate is best amino acid donor Escherichia coli 2-oxoglutarate + L-glutamate
-
 ?
L-glutamate + 2-oxoglutarate L-glutamate is best amino acid donor Escherichia coli B / ATCC 11303 2-oxoglutarate + L-glutamate
-
 ?
L-methionine + 2-oxoglutarate 1.0% of the activity with glutamate Escherichia coli L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
-
 ?
L-methionine + 2-oxoglutarate 1.0% of the activity with glutamate Escherichia coli B / ATCC 11303 L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
-
 ?
L-phenylalanine + 2-oxoglutarate
-
 Escherichia coli 2-oxo-3-phenylpropionic acid + L-glutamate i.e. phenylpyruvate ?
L-tryptophan + 2-oxoglutarate 11% of the activity with glutamate Escherichia coli 3-indole-2-oxopropionic acid + L-glutamate
-
 ?
L-tyrosine + 2-oxoglutarate 1.5 of the activity with glutamate Escherichia coli 3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate i.e. 4-hydroxyphenylpyruvate ?
L-tyrosine + 2-oxoglutarate 1.5 of the activity with glutamate Escherichia coli B / ATCC 11303 3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate i.e. 4-hydroxyphenylpyruvate ?

Subunits

Subunits Comment Organism
dimer 2 * 43000, SDS-PAGE Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8.5
-
 Escherichia coli