Extracts prepared from cultures of Bacillus subtilis, grown on maltose as the sole carbon source, lacked maltose phosphotransferase system activity. There was, however, evidence for a maltose phosphorylase activity, and such extracts also possessed both glucokinase and glucose phosphotransferase system activities. Maltose was accumulated by whole cells of B. subtilis by an energy-dependent mechanism. This uptake was sensitive to the effects of uncouplers, suggesting a role for the proton-motive force in maltose transport. Accumulation of maltose was inhibited in the presence of glucose, and there was no accumulation of maltose by a strain carrying the ptsl6 null-mutation. A strain carrying the temperature-sensitive ptsl1 mutation accumulated maltose normally at 37°C but, in contrast to the wild-type, was devoid of maltose transport activity at 47°C. The results indicate a role for the phosphotransferase system in the regulation of maltose transport activity in this organism. © 1992.
Tangney, M., Buchanan, C. J., Priest, F. G., & Mitchell, W. J. (1992). Maltose uptake and its regulation in Bacillus subtilis. FEMS Microbiology Letters, 97(1–2), 191–196. https://doi.org/10.1016/0378-1097(92)90385-2