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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.109(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster - Clostridium kluyveri butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.109(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster - Clostridioides difficile butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.109(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster i.e. crotonyl-CoA. NADH reduces beta-FAD of electron transferring flavoprotein, which bifurcates one electron to butanoyl-CoA dehydrogenase via FAD and the other to ferredoxin. Electron transferring flavoprotein (EtfAf) contains one FAD (alpha-FAD) in subunit alpha and a second FAD (beta-FAD) in subunit beta. The distance between the two isoalloxazine rings is 18 A°. The EtfAf-NAD+ complex structure reveals beta-FAD as acceptor of the hydride of NADH. The formed beta-FADH- is considered as the bifurcating electron donor. As a result of a domain movement, alpha-FAD is able to approach beta-FADH- by about 4 A and to take up one electron yielding a stable anionic semiquinone, alpha-FAD-/*, which donates this electron further to the FAD of butanoyl-CoA dehydrogenase BcdAf after a second domain movement. The remaining nonstabilized neutral semiquinone, beta-FADH*, immediately reduces ferredoxin. This electron flow from beta-FADH* to ferredoxin is only accomplished if the thermodynamically more favorable electron transfer to alpha-FAD-*. is prevented. Therefore, after the first electron transfer to alpha-FAD, a rotation is postulated of domain II toward the FAD binding site of butanoyl-CoA dehydrogenase BcdAf (based on spectroscopic and structural data). This conformational change, concomitantly, also reduces the distance between alpha-FAD-* and FAD from butanoyl-CoA dehydrogenase from about 30 to about 10 A. Thus, alpha-FAD embedded into the weakly associated domain II serves as a shuttle between the electron-donating beta-FADH- and the electron-accepting FAD of butanoyl-CoA dehydrogenase. Repetition leads to reduction of crotonyl-CoA Acidaminococcus fermentans butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.109(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster the enzyme couples the endergonic reduction of ferredoxin with NADH to the exergonic reduction of crotonyl-CoA to butanoyl-CoA Clostridium kluyveri butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.109(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster i.e. crotonyl-CoA. NADH reduces beta-FAD of electron transferring flavoprotein, which bifurcates one electron to butanoyl-CoA dehydrogenase via FAD and the other to ferredoxin. Electron transferring flavoprotein (EtfAf) contains one FAD (alpha-FAD) in subunit alpha and a second FAD (beta-FAD) in subunit beta. The distance between the two isoalloxazine rings is 18 A°. The EtfAf-NAD+ complex structure reveals beta-FAD as acceptor of the hydride of NADH. The formed beta-FADH- is considered as the bifurcating electron donor. As a result of a domain movement, alpha-FAD is able to approach beta-FADH- by about 4 A and to take up one electron yielding a stable anionic semiquinone, alpha-FAD-/*, which donates this electron further to the FAD of butanoyl-CoA dehydrogenase BcdAf after a second domain movement. The remaining nonstabilized neutral semiquinone, beta-FADH*, immediately reduces ferredoxin. This electron flow from beta-FADH* to ferredoxin is only accomplished if the thermodynamically more favorable electron transfer to alpha-FAD-*. is prevented. Therefore, after the first electron transfer to alpha-FAD, a rotation is postulated of domain II toward the FAD binding site of butanoyl-CoA dehydrogenase BcdAf (based on spectroscopic and structural data). This conformational change, concomitantly, also reduces the distance between alpha-FAD-* and FAD from butanoyl-CoA dehydrogenase from about 30 to about 10 A. Thus, alpha-FAD embedded into the weakly associated domain II serves as a shuttle between the electron-donating beta-FADH- and the electron-accepting FAD of butanoyl-CoA dehydrogenase. Repetition leads to reduction of crotonyl-CoA Acidaminococcus fermentans DSM 20731 butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.109(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster - Clostridioides difficile DSM 1296T butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.109(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation Acidaminococcus fermentans butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.109(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation Acidaminococcus fermentans DSM 20731 butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.109(E)-but-2-enoyl-CoA + 2 NADH + oxidized ferredoxin iron-sulfur cluster the bifurcating butyryl-CoA dehydrogenase catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH Clostridioides difficile butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.109(E)-but-2-enoyl-CoA + 2 NADH + oxidized ferredoxin iron-sulfur cluster the bifurcating butyryl-CoA dehydrogenase catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH Clostridioides difficile DSM 1296T butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster - ?
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