Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

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.

Author: Francois, Jean, Booth, Ian R., Pearce, Amanda K., Crimmins, Kay, Groussac, Evelyne, Hewlins, Michael J.E., Dickinson, J. Richard, Brown, Alistair J.P.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2001
France, Fermentation, Carbon

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


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.

Author: Booth, Ian R., Pearce, Amanda K., Brown, Alistair J.P.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2001
Food, Cells (Biology), Protection and preservation, Growth, Food preservation, Cells, Benzoic acid

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


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.

Author: Hewlins, Michael J.E., Dickinson, J. Richard, Sobanski, Michael A.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
Analysis, Glucose metabolism, Isomerases

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: United Kingdom, Statistical Data Included, Research, Physiological aspects, Cytochemistry, Yeast, Yeast (Food product), Protein kinases, Glycolysis, Genetic aspects, Saccharomyces
Similar abstracts:
  • Abstracts: The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae
  • Abstracts: Improved secretion of native human insulin-like growth factor 1 from gas1 mutant Saccharomyces cerevisiae cells
  • Abstracts: The adnA transcriptional factor affects persistence and spread of Pseudomonas fluorescens under natural field conditions
  • Abstracts: Cytochrome C(sub 550) is an essential component of the quinoprotein ethanole oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome C(sub 55) and an adjacent acetaldehyde dehydrogenase
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.