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Literature summary for 2.6.1.1 extracted from

  • Hayashi, H.; Kagamiyama, H.
    Reaction of aspartate aminotransferase with L-erythro-3-hydroxyaspartate: involvement of Tyr70 in stabilization of the catalytic intermediates (1995), Biochemistry, 34, 9413-9423.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
T70F nearly no activity with L-erythro-3-hydroxyaspartate, in opposite to the wild-type, altered reaction kinetics due to inability to stabilize the reaction quinonoid intermediate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Escherichia coli
additional information
-
additional information wild-type and mutants 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
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate mechanism Escherichia coli
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate intermediate formation Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
Escherichia coli oxaloacetate + L-glutamate
-
?
L-aspartate + 2-oxoglutarate
-
Escherichia coli oxaloacetate + L-glutamate
-
r
L-erythro-3-hydroxyaspartate + 2-oxoglutarate high stabilization of the quinonoid intermediate formed by L-erythro-3-hydroxyaspartate and pyridoxal 5'-phosphate at the active site via Tyr70, kinetic analysis Escherichia coli erythro-3-hydroxy-2-oxoaspartate + L-glutamate
-
?
L-erythro-3-hydroxyaspartate + 2-oxoglutarate wild-type, no activity with mutant T70F Escherichia coli erythro-3-hydroxy-2-oxoaspartate + L-glutamate
-
?