Isocitrate dehydrogenases and oxoglutarate dehydrogenase activities of baker's yeast grown in a variety of hypoxic conditions.
The activities of isocitrate dehydrogenase (NAD), isocitrate dehydrogenase (NADP) and oxoglutarate dehydrogenase have been investigated in Saccharomyces cerevisiae grown in a variety of aerobic and hypoxic conditions, the latter including oxygen deprivation, high glucose concentration, addition of inhibitors of mitochondrial protein synthesis, respiratory inhibition by azide, and impaired respiration mutants. All hypoxic conditions led to a marked decrease of oxoglutarate dehydrogenase and significant decreases of the two isocitrate dehydrogenases. According to its kinetic properties, the NAD-isocitrate dehydrogenase will not be operative in hypoxia "in vivo". From these and other related facts it is concluded that hypoxic conditions in yeast generally lead to a splitting of the tricarboxylic acid cycle and that glutamate synthesis in these conditions takes place through the coupling of the NADP-linked isocitrate and glutamate dehydrogenases.
D000332:Aerobiosis; D000693:Anaerobiosis; D001386:Azides / Q000494:pharmacology; D002701:Chloramphenicol / Q000494:pharmacology; D005632:Fructose / Q000494:pharmacology; D005690:Galactose / Q000494:pharmacology; D005947:Glucose / Q000494:pharmacology; D007521:Isocitrate Dehydrogenase / Q000378:metabolism*; D007655:Ketoglutarate Dehydrogenase Complex / Q000378:metabolism*; D007658:Ketone Oxidoreductases / Q000378:metabolism*; D008358:Mannose / Q000494:pharmacology; D009154:Mutation; D010118:Oxytetracycline / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000201:enzymology*
D001386:Azides; D005632:Fructose; D002701:Chloramphenicol; D007521:Isocitrate Dehydrogenase; D007658:Ketone Oxidoreductases; D007655:Ketoglutarate Dehydrogenase Complex; D005947:Glucose; D008358:Mannose; D010118:Oxytetracycline; D005690:Galactose