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Partial purification and characterization of succinyl-CoA synthetase from Saccharomyces cerevisiae

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Abstract

Succinyl-CoA synthetase from Saccharomyces cerevisiae was partially purified (20-fold) with a yield of 44%. The Michaelis-Menten constants were determined: K m (succinate)=17mm; K m (ATP)=0.13mm; K m (CoA)=0.03mm. 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.

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Schwartz, H., Steitz, H.O. & Radler, F. Partial purification and characterization of succinyl-CoA synthetase from Saccharomyces cerevisiae . Antonie van Leeuwenhoek 49, 69–78 (1983). https://doi.org/10.1007/BF00457881

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