[Study of the NADH and NADPH-ferredoxin oxidoreductase activities in Clostridium acetobutylicum].
The NADH and NADPH-ferredoxin oxidoreductase have been studied in Clostridium acetobutylicum. Acetyl-CoA is an obligatory activator of NADH-ferredoxin reductase activity and NADH a competitive inhibitor of ferredoxin-NAD+ reductase activity. These regulations are the same when C. acetoburylicum moves from 'butylic-type metabolism' to 'butyric-type metabolism'; this demonstrates that NADH-ferredoxin oxidoreductase cna, through its reversible action, meet the very different cell needs imposed by these two types of culture. The physiological function of the clostridial NADPH-ferredoxin oxidoreductase was anabolic as it has been with other clostridia.
D000105:Acetyl Coenzyme A / Q000378:metabolism; D003013:Clostridium / Q000201:enzymology* / Q000378:metabolism; D004789:Enzyme Activation; D005287:Ferredoxin-NADP Reductase / Q000378:metabolism; D005288:Ferredoxins / Q000378:metabolism; D005947:Glucose / Q000378:metabolism; D009243:NAD / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D009249:NADP / Q000378:metabolism; D011773:Pyruvates / Q000378:metabolism
D005288:Ferredoxins; D011773:Pyruvates; D009243:NAD; D009249:NADP; D000105:Acetyl Coenzyme A; D005287:Ferredoxin-NADP Reductase; D009247:NADH, NADPH Oxidoreductases; D005947:Glucose
Etude des activités NADH et NADPH-ferrédoxine oxydoréductasiques chez Clostridium acetobutylicum