Literature summary for 1.3.5.1 extracted from

Schnorpfeil, M.; Janausch, I.G.; Biel, S.; Kroger, A.; Unden, G.
Generation of a proton potential by succinate dehydrogenase of Bacillus subtilis functioning as a fumarate reductase (2001), Eur. J. Biochem., 268, 3069-3074.

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Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-

General Information

General Information	Comment	Organism
physiological function	fumarate reduction by NADH is catalyzed by an electron transport chain consisting of NADH dehydrogenase NADH:menaquinone reductase, menaquinone, and succinate dehydrogenase operating in the reverse direction, i.e. menaquinol:fumarate reductase. In sdh or aro mutant strains, which lack succinate dehydrogenase or menaquinone, respectively, the activity of fumarate reduction by NADH is missing. The membrane fraction of a mutant lacking functional sdh genes catalyzes fumarate reduction by NADH or 2,3-dimethyl-1,4-naphthoquinol with less than 7% of the wild-type activities. In resting cells fumarate reduction requires glycerol or glucose as the electron donor, which presumably supply NADH for fumarate reduction	Bacillus subtilis

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Release 2023.1 (January 2023)