Literature summary for 1.4.3.16 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.

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Protein Variants

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

Organism

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

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

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Release 2023.1 (January 2023)