Literature summary for 1.4.3.16 extracted from

Tedeschi, G.; Negri, A.; Mortarino, M.; Ceciliani, F.; Simonic, T.; Faotto, L.; Ronchi, S.
L-Aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate:fumarate oxidoreductase activity (1996), Eur. J. Biochem., 239, 427-433.

Search for more literature for 1.4.3.16

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	fumarate reductase in anaerobic conditions	-

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	fumarate or succinate can be electron acceptor instead of O2	Escherichia coli	oxaloacetate + NH3 + H2O2	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
2.6	-	L-aspartate	oxygen electron acceptor	Escherichia coli
5.55	-	L-aspartate	fumarate electron acceptor	Escherichia coli

Cofactor

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)