Inactivation of the galactose transport system in Saccharomyces cerevisiae
- 27 October 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 207 (2), 258-261
- https://doi.org/10.1016/0014-5793(86)81500-9
Abstract
The galactose transport system of Saccharomyces cerevisiae consists of one component which shows a Km value of approx. 4mM in growing cells. A rapid and irreversible inactivation of this transport is detected on impairment of protein synthesis. This inactivation shows the following characteristics: (i) it is due to changes in the Km and Vmax of the transport system; (ii) it follows first-order kinetics; (iii) it is an energy-dependent process and is stimulated by the presence of an exogenous carbon source; (iv) fermentable sub-dependent process and is stimulated by the presence of an exogenous carbon source; (iv) fermentable substrates stimulate inactivation more efficiently than non-fermentable substrates.Keywords
This publication has 17 references indexed in Scilit:
- Catabolite Inactivation of the Glucose Transport System in Saccharomyces cerevisiaeMicrobiology, 1986
- Identification of two forms of the maltose transport system in Saccharomyces cerevisiae and their regulation by catabolite inactivationBiochimica et Biophysica Acta (BBA) - Biomembranes, 1985
- Involvement of kinases in glucose and fructose uptake by Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences, 1983
- Energy Requirements for Maltose Transport in YeastEuropean Journal of Biochemistry, 1977
- Catabolite inactivation of the galactose uptake system in yeast.Journal of Biological Chemistry, 1977
- Energy metabolism of Saccharomyces cerevisiae discrepancy between ATP balance and known metabolic functionsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1976
- Biochemical correlates of respiratory deficiencyArchives of Biochemistry and Biophysics, 1966
- On the Evaluation of the Constants Vm and KM in Enzyme ReactionsScience, 1952
- On the Evaluation of the Constants
V
m
and
K
M
in Enzyme ReactionsScience, 1952