An F1-ATPase-defective mutant of Escherichia coil K-12, strain TBLA-1, showing an enhanced pyruvic acid productivity compared with its parental strain W1485lip2, was characterized physiologically to elucidate the mechanisms of the enhancement in productivity. Cells of strain TBLA-1 producing pyruvic acid showed a higher rate of the oxygen consumption and a higher b-type cytochromes content than cells of strain W1485lip2. The activities of the phosphotransferase system for glucose uptake measured in terms of the level of phosphoenolpyruvate-dependent phosphorylation of methyl α-D-glucopyranoside and 2-deoxy-D-glucose using toluenized cells were higher in strain TBLA-1 than in strain W1485lip2. Among the activities of all the glycolytic enzymes, those of phosphoglycerate kinase and pyruvate kinase-I were found to be higher in strain TBLA-1 than in strain W1485lip2 during the logarithmic growth phase. These characteristics of strain TBLA-1 are discussed in relation to its enhanced pyruvic acid productivity.
Yokota, A., Henmi, M., Takaoka, N., Hayashi, C., Takezawa, Y., Fukumori, Y., & Tomita, F. (1997). Enhancement of glucose metabolism in a pyruvic acid-hyperproducing Escherichia coli mutant defective in F1-ATPase activity. Journal of Fermentation and Bioengineering, 83(2), 132–138. https://doi.org/10.1016/S0922-338X(97)83571-4