title: Evidence that a low-affinity sucrose phosphotransferase activity in Streptococcus mutans GS-5 is a high-affinity trehalose uptake system.
abstract: 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.
authors.affiliation: Department of Biology, Boston University, Massachusetts 02215.
authors.forename: F
authors.initials: F
authors.lastname: Poy
authors.forename: G R
authors.initials: GR
authors.lastname: Jacobson
mesh_terms: 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*
chemical_list: D004187:Disaccharides; D013395:Sucrose; D014199:Trehalose; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System