Pyruvate decarboxylase catalyzes decarboxylation of branched-chain 2-oxo acids but is not essential for fusel alcohol production by Saccharomyces cerevisiae

Article Abstract:

Research was conducted to examine the role of pyruvate decarboxylase in the production of fusel alcohols by Saccharomyces cerevisiae which harbors three structural genes, PDC1, PDC5 and PDC6. Wild-type S cerevisiae and an isogenic pyruvate decarboxylase-negative strain were grown on ethanol with a mixture of leucine, isoleucine and valine as the nitrogen source. Results showing the production of three corresponding fusel alcohols in both strains indicate that decarboxylation of branched-chain 2-oxo acids is not an important step in fusel alcohol production.

Alcohol, Ethanol

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Metabolic responses of pyruvate decarboxylase-negative Saccharomyces cerevisiae to glucose excess

Article Abstract:

Microbiological research shows that the enzyme pyruvate decarboxylase of the organism Saccharomyces cerevisiae is not quickly deactivated in the presence of high glucose levels. The pyruvate dehydrogenase complex appears to be regulated by another process, as yet unidentified. The organism exhibits high glycolytic fluxes and requires high levels of reoxidation of cytosolic NADH via pyruvate decarboxylase and alcohol dehydrogenase.

Yeast fungi, Yeasts (Fungi)

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Effects of pyruvate decarboxylase overproduction on flux distribution at the pyruvate branch point in Saccharomyces cerevisiae

Article Abstract:

A study was conducted to examine the influence of pyruvate decarboxylase overproduction on flux distributions in Saccharomyces cerevisiae. Maximum glycolytic capacity was determined by harvesting samples using centrifugation while glucose was obtained with a glucose oxidase kit. Results showed that the pyruvate decarboxylase overproduction had no effect on the fermentative capability of S. cerevisiae respiratory cultures.

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