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Literature summary extracted from

  • Yagi, T.; Toyosato, M.; Soda, K.
    Crystalline aspartate aminotransferase from Pseudomonas striata (1976), FEBS Lett., 61, 34-37.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.1 concentrated protein solution, potassium phosphate 0,01 M, pH 7.2, 0.01 mM pyridoxal 5'-phosphate, ammonium sulfate Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.1 80000
-
 meniscus depletion sedimentation equilibrium method Pseudomonas putida

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 Pseudomonas putida enzyme plays the most important role in amino acid metabolism oxaloacetate + L-glutamate
-
 ?
2.6.1.1 L-aspartate + 2-oxoglutarate Pseudomonas putida IFO 12996 enzyme plays the most important role in amino acid metabolism oxaloacetate + L-glutamate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.1 Pseudomonas putida
-
-
-
2.6.1.1 Pseudomonas putida IFO 12996
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.1
-
 Pseudomonas putida

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6.1.1 additional information
-
-
 Pseudomonas putida
2.6.1.1 45.15
-
 purified enzyme Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.1 L-aspartate + 2-oxoglutarate 34% of the activity with glutamate Pseudomonas putida oxaloacetate + L-glutamate
-
 ?
2.6.1.1 L-aspartate + 2-oxoglutarate enzyme plays the most important role in amino acid metabolism Pseudomonas putida oxaloacetate + L-glutamate
-
 ?
2.6.1.1 L-aspartate + 2-oxoglutarate 34% of the activity with glutamate Pseudomonas putida IFO 12996 oxaloacetate + L-glutamate
-
 ?
2.6.1.1 L-aspartate + 2-oxoglutarate enzyme plays the most important role in amino acid metabolism Pseudomonas putida IFO 12996 oxaloacetate + L-glutamate
-
 ?
2.6.1.1 L-cysteine sulfinic acid + 2-oxoglutarate 21% of the activity with L-glutamate Pseudomonas putida 2-oxo-3-sulfinopropionic acid + L-glutamate
-
 ?
2.6.1.1 L-cysteine sulfinic acid + 2-oxoglutarate 21% of the activity with L-glutamate Pseudomonas putida IFO 12996 2-oxo-3-sulfinopropionic acid + L-glutamate
-
 ?
2.6.1.1 L-glutamate + 2-oxoglutarate L-glutamate is best amino acid donor Pseudomonas putida 2-oxoglutarate + L-glutamate
-
 ?
2.6.1.1 L-glutamate + 2-oxoglutarate L-glutamate is best amino acid donor Pseudomonas putida IFO 12996 2-oxoglutarate + L-glutamate
-
 ?
2.6.1.1 L-phenylalanine + 2-oxoglutarate 6.9% of the activity with glutamate Pseudomonas putida 2-oxo-3-phenylpropionic acid + L-glutamate i.e. phenylpyruvate ?
2.6.1.1 L-tyrosine + 2-oxoglutarate 1.2% of the activity with glutamate Pseudomonas putida 3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate i.e. 4-hydroxyphenylpyruvate ?
2.6.1.1 additional information substrate specificity Pseudomonas putida ?
-
 ?
2.6.1.1 additional information substrate specificity Pseudomonas putida IFO 12996 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.6.1.1 dimer
-
 Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.1 30
-
 assay at Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.1 8 8.3 2 reaction methods Pseudomonas putida
2.6.1.1 8.3 8.6
-
 Pseudomonas putida