Pyruvate kinase (Pyk1) levels influence both the rate and direction of carbon flux in yeast under fermentative conditions
Article Abstract:
Pyruvate kinase (Pyk1) levels have been found to influence the direction and rate of carbon flux in yeast under fermentation conditions. Contrasting views of glycolytic regulation in yeast were studied by looking at the effects on yeast physiology of disrupting transactional and post-transcriptional regulation of the PFK2, PYK1 and PFK1 genes and changing Pfk1 and Pyk1 levels. Gene regulation seems to play a minor role in control of glycolytic flux in fermentation conditions.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2001
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Genetic manipulation of 6-phosphofructo-1-kinase and fructose 2,6-bisphosphate levels affects the extent to which benzoic acid inhibits the growth of Saccharomyces cerevisiae
Article Abstract:
Genetic manipulation of fructose 2,6-bisphosphate and 6-phosphofructo-1-kinase (PF1K) levels, which is activated by the former, has been found to affect the extent to which benzoic acid inhibits Saccharomyces cerevisiae growth. A causal relationship exists between gloycoloysis inhibition and benzoic acid antimicrobial effects. Resistance was increased by elevating PF1K levels, but was not dependent on optimum glycolytic flux.The mechanisms by which the benzoic acid acts as a weak acid preservative in food to inhibit the growth of S. cerevisiae were investigated.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2001
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In Saccharomyces cerevisiae deletion of phosphoglucose isomerase can be suppressed by increased activities of enzymes of the hexose monophosphate pathway
Article Abstract:
Examination of the glucose metabolism of Saccharomyces cerevisiae mutants lacking phosphoglucose isomerase by 13C NMR spectroscopy reveals that increase in carbon flux via the hexose monophosphate pathway inhibits the glycolytic defect in a spg29 mutant. Bypass mutants exhibit high activities of NAD- and NADP-dependent glutamate dehydrogenase and enzymes of the hexose monophosphate pathway.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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