Overproduction of glycolytic enzymes in yeast
Article first published online: 29 JAN 2004
Copyright © 1989 John Wiley & Sons Ltd.
Volume 5, Issue 4, pages 285–290, July/August 1989
How to Cite
Schaaff, I., Heinisch, J. and Zimmermann, F. K. (1989), Overproduction of glycolytic enzymes in yeast. Yeast, 5: 285–290. doi: 10.1002/yea.320050408
- Issue published online: 29 JAN 2004
- Article first published online: 29 JAN 2004
- Manuscript Revised: 16 MAR 1989
- Manuscript Received: 11 NOV 1988
- Saccharomyces cerevisiae;
- metabolic flux;
- ethanol production
Eight different enzyymes for glycolysis and alcoholic fermentation were overproduced in a common Saccharomyces cerevisiae strain by placing their genes on multicopy vectors. The specific enzyme activities were increased between 3·7-and 13·9-fold above the wild-type level. The overproduction of the different glycolytic enzymes had no effect on the rate of ethanol formation, even with those enzymes that catalyse irreversible steps: hexokinase, phosphofructokinase and pyruvate kinase. Also the simultaneous increase in the activities of pairs of enzymes such as pyruvate kinase and phosphofructokinase or pyruvate decarboxylase and alcohol dehyrogenase, did not increase the rate of ethanol production. The levels of key glycolytic metabolites were also normal, compared to the reference strain.