Literature summary for 1.4.3.16 extracted from

Tedeschi, G.; Ronchi, S.; Simonic, T.; Treu, C.; Mattevi, A.; Negri, A.
Probing the active site of L-aspartate oxidase by site-directed mutagenesis: Role of basic residues in fumarate reduction (2001), Biochemistry, 40, 4738-4744.

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Protein Variants

Protein Variants	Comment	Organism
H244A	binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate	Escherichia coli
H244S	binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate	Escherichia coli
H351A	binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate	Escherichia coli
H351S	binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate	Escherichia coli
R386L	binds substrate analogues with higher dissociation constants and presens lower kcat/Km values in the reduction of fumarate	Escherichia coli

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	-	?

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Escherichia coli

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Release 2023.1 (January 2023)