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Literature summary for 2.6.1.1 extracted from

  • Graindorge, M.; Giustini, C.; Kraut, A.; Moyet, L.; Curien, G.; Matringe, M.
    Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms (2014), J. Biol. Chem., 289, 3198-3208.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.017
-
oxaloacetate pH 8.0, 30°C Sinorhizobium meliloti

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti Q02635 bifunctional aspartate aminotransferase and aspartate:prephenate aminotransferase, EC 2.6.1.79
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxaloacetate + L-glutamate
-
Sinorhizobium meliloti L-aspartate + 2-oxoglutarate
-
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Synonyms

Synonyms Comment Organism
aatA
-
Sinorhizobium meliloti
aspartate aminotransferase A
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Sinorhizobium meliloti

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
205
-
oxaloacetate pH 8.0, 30°C Sinorhizobium meliloti