Listeria monocytogenes transported glucose by a high-affinity phosphoenolpyruvate-dependent phosphotransferase system and a low-affinity proton motive force-mediated system. The low-affinity system (K(m) = 2.9 mM) was inhibited by 2-deoxyglucose and 6-deoxyglucose, whereas the high-affinity system (K(m) = 0.11 mM) was inhibited by 2-deoxyglucose and mannose but not 6-deoxyglucose. Cells and vesicles artificially energized with valinomycin transported glucose or 2-deoxyglucose at rates greater than those of de- energized cells, indicating that a membrane potential could drive uptake by the low-affinity system.
|Original language||English (US)|
|Number of pages||4|
|Journal||Applied and environmental microbiology|
|State||Published - Feb 1 1997|
ASJC Scopus subject areas
- Food Science
- Applied Microbiology and Biotechnology