Evidence that a low-affinity sucrose phosphotransferase activity in Streptococcus mutans GS-5 is a high-affinity trehalose uptake system.
High-affinity sucrose uptake in the oral pathogen Streptococcus mutans is mediated by the phosphoenolpyruvate-dependent phosphotransferase system. In this report, we provide evidence that a lower-affinity sucrose phosphotransferase system in S. mutans GS-5, previously described by others, is in fact a high-affinity trehalose uptake system that also recognizes sucrose as a substrate.
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Department of Biology, Boston University, Massachusetts 02215.
Jacobson
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GR
D001693:Biological Transport, Active; D004187:Disaccharides / Q000378:metabolism*; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism*; D010766:Phosphorylation; D013295:Streptococcus mutans / Q000378:metabolism*; D013395:Sucrose / Q000378:metabolism*; D014199:Trehalose / Q000378:metabolism*
D004187:Disaccharides; D013395:Sucrose; D014199:Trehalose; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System