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Overproduction of glycolytic enzymes in yeast
Author(s) -
Schaaff Ine,
Heinisch Jürgen,
Zimmermann Friedrich K.
Publication year - 1989
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320050408
Subject(s) - phosphofructokinase , pyruvate decarboxylase , pyruvate kinase , glycolysis , biochemistry , biology , hexokinase , enzyme , overproduction , saccharomyces cerevisiae , yeast , ethanol fermentation , fermentation , alcohol dehydrogenase
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.