Literature summary for 1.3.5.1 extracted from

Schroder, I.; Gunsalus, R.P.; Ackrell, B.A.; Cochran, B.; Cecchini, G.
Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis (1991), J. Biol. Chem., 266, 13572-13579.

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Protein Variants

Protein Variants	Comment	Organism
C247	mutation in flavoprotein subunit FrdA. Increase in fumarate reduction rate, slight increase in succinate oxidation. Residue C247 of FrdA is responsible for the N-ethylmaleimide sensitivity shown by fumarate reductase but is not required for catalytic activity or the tight-binding of oxalacetate	Escherichia coli
H232S	mutation in flavoprotein subunit FrdA. Decrease in fumarate reduction, strong decrease in succinate oxidation. Residue H232 is the general acid-base catalyst	Escherichia coli
R248H	mutation in flavoprotein subunit FrdA. Strong decrease both in fumarate reduction and in succinate oxidation	Escherichia coli
R248L	mutation in flavoprotein subunit FrdA. Strong decrease both in fumarate reduction and in succinate oxidation	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
fumarate + menaquinol-6	-	Escherichia coli	succinate + menaquinone-6	-	r
fumarate + reduced benzyl viologen	-	Escherichia coli	succinate + benzyl viologen	-	r
additional information	enzyme also accepts artificial electron acceptors, reaction of EC 1.3.99.1	Escherichia coli	?	-	?
succinate + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone	-	Escherichia coli	fumarate + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinol	-	r
succinate + phenazine methosulfate	-	Escherichia coli	fumarate + reduced phenazine methosulfate	-	?

Cofactor

Cofactor	Comment	Organism	Structure
2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone	-	Escherichia coli
benzyl viologen	-	Escherichia coli
menaquinol-6	-	Escherichia coli
phenazine methosulfate	-	Escherichia coli

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Release 2023.1 (January 2023)