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Literature summary for 2.6.1.1 extracted from

  • Birolo, L.; Arnone, M.I.; Cubellis, M.V.; Andreotti, G.; Nitti, G.; Marino, G.; Sannia, G.
    The active site of Sulfolobus solfataricus aspartate aminotransferase. (1991), Biochim. Biophys. Acta, 1080, 198-204.
    View publication on PubMed
Search for more literature for 2.6.1.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.25
-
 L-aspartate 60°C Saccharolobus solfataricus
140
-
 L-alanine 60°C Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus P14909
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine + 2-oxoglutarate activity is not affected by the presence of formate Saccharolobus solfataricus pyruvate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate aspartate aminotransferase from Sulfolobus solfataricus does not possess any arginine residue exposed to chemical modifications responsible for the binding of omega-carboxylate of the substrates Saccharolobus solfataricus oxaloacetate + L-glutamate
-
 ?
L-cysteine sulfinic acid + 2-oxoglutarate
-
 Saccharolobus solfataricus 2-oxo-3-sulfinopropionic acid + L-glutamate
-
 ?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Saccharolobus solfataricus