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Literature summary for 2.6.1.42 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
0.045
-
4-methyl-2-oxopentanoate pH 8.0, 30°C Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp. P54691 bifunctional branched-chain aminotransferase and aspartate:prephenate aminotransferase, EC 2.6.1.79
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methyl-2-oxopentanoate + L-glutamate
-
Synechocystis sp. L-leucine + 2-oxoglutarate
-
?

Synonyms

Synonyms Comment Organism
IlvE
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Synechocystis sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
70
-
4-methyl-2-oxopentanoate pH 8.0, 30°C Synechocystis sp.