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Literature summary for 2.6.1.1 extracted from

  • Kamitori, S.; Hirotsu, K.; Higuchi, T.; Kondo, K.; Inoue, K.; Kuramitsu, S.; Kagamiyama, H.; Higuchi, Y.; Yasuoka, N.; Kusunoki, M.; Matsuura, Y.
    Overproduction and preliminary X-ray characterization of aspartate aminotransferase from Escherichia coli (1987), J. Biochem., 101, 813-816.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression from plasmid in strain JM103 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop method, protein solution: 30 mg/ml, 10 mM potassium phosphate, pH 7.0, 0.01 mM pyridoxal 5'-phosphate, 1 mM EDTA, 2 mM succinate, 0.3 mM azide, reservoir solution: same composition as protein solution, contains no protein but polyethylene glycol 4000, 11-17% w/v, 20°C, stepwise addition of protein solution, X-ray diffraction analysis 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
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinantly overexpressed enzyme Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
232
-
purified recombinant enyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
Escherichia coli oxaloacetate + L-glutamate
-
?

Subunits

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

Cofactor

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