Literature summary for 1.3.5.1 extracted from

Blaut, M.; Whittaker, K.; Valdovinos, A.; Ackrell, A.C.; Gunsalus, R.P.; Cecchini, G.
Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin (1989), J. Biol. Chem., 264, 13599-13604.

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Protein Variants

Protein Variants	Comment	Organism
H44C	the mutation allows cell growth in glycerol/fumarate medium at a 4fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 38% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex	Escherichia coli
H44R	the mutation does not allow cells to grow anaerobically on glycerol and fumarate, the substitution produces an inactive complex	Escherichia coli
H44S	the mutation allows cell growth in glycerol/fumarate medium at a 4fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 32% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex	Escherichia coli
H44Y	the mutation allows cell growth in glycerol/fumarate medium at a 7fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 17% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	fumarate reductase	-

Cofactor

Cofactor	Comment	Organism	Structure
FAD	role in succinate oxidation	Escherichia coli

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Release 2023.1 (January 2023)