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Literature summary for 2.6.1.1 extracted from

  • Herold, M.; Kirschner, K.
    Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: characterization of a monomeric intermediate (1990), Biochemistry, 29, 1907-1913.
    View publication on PubMed

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

Renatured (Commentary)

Renatured (Comment) Organism
reversible dissociation and unfolding of the dimeric enzyme by guanidine hydrochloride 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