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Literature summary for extracted from

  • Mortarino, M.; Negri, A.; Tedeschi, G.; Simonic, T.; Duga, S.; Gassen, H.G.; Ronchi, S.
    L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition (1996), Eur. J. Biochem., 239, 418-426.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information mutant reduces affinity to FAD Escherichia coli


Organism UniProt Comment Textmining
Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
overexpression in Escherichia coli Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + H2O + O2
Escherichia coli oxaloacetate + NH3 + H2O2


Cofactor Comment Organism Structure
FAD 1 mol of FAD covalently bound per mol of enzyme Escherichia coli