2022/08/26 by Pranas Grigaitis, Bas Teusink · 5 citations
Biochemistry, Genetics and Molecular Biology · Engineering · #Fungal and yeast genetics research #Microbial Metabolic Engineering and Bioproduction #Biofuel production and bioconversion
paper · pdf · doi:10.1002/1873-3468.14484
Microorganisms, including the budding yeast Saccharomyces cerevisiae, express glycolytic proteins to a maximal capacity that (largely) exceeds the actual flux through the enzymes, especially at low growth rates. An open question is if this apparent expression level is really an overcapacity, or maintains the (optimal) enzyme capacity needed to carry flux at (very) low substrate availability. Here, we use computational modelling to suggest that yeast maintains a genuine excess of glycolytic enzymes at low specific growth rates. During fast fermentative growth at high glucose levels, the observed expression of the glycolytic enzymes matched the predicted optimal levels. We suggest that the excess glycolytic capacity at low glucose levels is a preparatory strategy in the adaptation to sugar fluctuations in the environment.