Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1981 May;129(3):216-20.
doi: 10.1007/BF00425254.

Concentration of metabolites and the regulation of phosphofructokinase and fructose-1,6-bisphosphatase in Saccharomyces cerevisiae

J J Foy, J K Bhattacharjee

Concentration of metabolites and the regulation of phosphofructokinase and fructose-1,6-bisphosphatase in Saccharomyces cerevisiae

J J Foy et al. Arch Microbiol. 1981 May.

Abstract

The intracellular levels of adenosine triphosphate and several glycolytic intermediates were determined in Saccharomyces cerevisiae in relation to the presence of the metabolically antagonistic enzymes phosphofructokinase and fructose-1,6-bisphosphatase. Phosphofructokinase is synthesized constitutively in cells grown in the presence of glucose and fructose-1,6-bisphosphatase derepression occurs upon the exhaustion of glucose from the growth medium. Transcriptional regulation of fructose-1,6-bisphosphatase was suggested based on experiments with wild type cells using 8-hydroxyquinoline, a known inhibitor of nuclear transcription, and with the S. cerevisiae mutant strain A364A (ts-136) blocked in the transport of nuclear RNA at non-permissive temperature. The level of phosphofructokinase was reduced more than 25-fold under conditions of high citrate accumulation in an aconitase-less, glutamate requiring mutant strain, MO-1-9B. There was a rapid decrease in the levels of adenosine triphosphate and fructose-1,6-bisphosphate at the end of log-phase of culture growth when both fructose-1,6-bisphosphatase and phosphofructokinase were present in the cells simultaneously. The changes in the levels of key glycolytic intermediates, but not the changes in adenosine triphosphate, during the simultaneous presence of these two enzymes, can be explained without involving any futile cycling.

PubMed Disclaimer

Similar articles

See all similar articles

References

    1. Mol Gen Genet. 1978 Feb 27;159(3):329-35 - PubMed
    1. Biochem J. 1965 Oct;97(1):284-97 - PubMed
    1. Appl Microbiol. 1975 Nov;30(5):713-21 - PubMed
    1. J Bacteriol. 1977 Feb;129(2):978-82 - PubMed
    1. Biochim Biophys Acta. 1976 Sep 13;440(3):661-74 - PubMed

Publication types

MeSH terms

LinkOut - more resources