6533b7dafe1ef96bd126eca0
RESEARCH PRODUCT
Partial purification and characterization of succinyl-CoA synthetase from Saccharomyces cerevisiae
H O SteitzF RadlerH Schwartzsubject
Saccharomyces cerevisiaeSuccinic AcidCatabolite repressionSaccharomyces cerevisiaeMicrobiologyAdenosine TriphosphateCoenzyme A LigasesSuccinate-CoA LigasesAnaerobiosisMolecular BiologyGel electrophoresischemistry.chemical_classificationChromatographybiologyorganic chemicalsSuccinyl coenzyme A synthetaseTemperatureSuccinatesSuccinate-CoA LigasesGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationYeastAmino acidMolecular WeightKineticsBiochemistrychemistrybacteriaFermentationdescription
Succinyl-CoA synthetase from Saccharomyces cerevisiae was partially purified (20-fold) with a yield of 44%. The Michaelis-Menten constants were determined: Km (succinate) = 17 mM; Km (ATP) = 0.13 mM; Km (CoA) = 0.03 mM. The succinyl-CoA synthetase has a molecular weight of about 80000 dalton (as determined by polyacrylamide gradient gel electrophoresis). The pH optimum is at 6.0. During fermentation the activity of succinyl-CoA synthetase is lower than in aerobically grown yeast cells. The presence of succinyl-CoA synthetase in fermenting yeasts may be regarded as an indication for the oxidative formation of succinate. In fermenting yeast cells succinyl-CoA synthetase is repressed by glucose if ammonium sulphate serves as nitrogen source. This catabolite repression is not observed with disaccharides or when amino acids are used as nitrogen source.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1983-04-01 | Antonie van Leeuwenhoek |