[Enzymatic study of citrate-isocitrate accumulation in yeast with glucose as the carbon source].
The connection between the kinetics of citrate-isocitrate overproduction by Saccharomycopsis lipolytica in glucose media and the specific activities of the enzymes being related to overproduction has been investigated. The specific activities of citrate synthase, aconitate hydratase, NAD+-linked and NADP+-linked isocitrate dehydrogenase decline significantly after exhaustion of the nitrogen source, whereas the activity of the pyruvate carboxylase remains relatively constant and corresponds to changes of the production rate. The results are compared with those obtained by fermentations in n-alkane media and discussed in relation to mechanisms of overproduction.
D000154:Aconitate Hydratase / Q000378:metabolism; D001203:Ascomycota / Q000201:enzymology*; D002950:Citrate (si)-Synthase / Q000378:metabolism; D002951:Citrates / Q000096:biosynthesis*; D019343:Citric Acid; D005947:Glucose / Q000378:metabolism*; D007521:Isocitrate Dehydrogenase / Q000378:metabolism; D007523:Isocitrates / Q000096:biosynthesis*; D007700:Kinetics; D011766:Pyruvate Carboxylase / Q000378:metabolism; D012442:Saccharomycopsis / Q000201:enzymology*
D002951:Citrates; D007523:Isocitrates; D019343:Citric Acid; D007521:Isocitrate Dehydrogenase; D002950:Citrate (si)-Synthase; D000154:Aconitate Hydratase; D011766:Pyruvate Carboxylase; D005947:Glucose
Enzymatische Untersuchungen zur Citrat-Isocitrat-Akkumulation bei Hefen mit Glucose als C-Quelle.