title: A phosphoenolpyruvate-dependent phosphotransferase system is the principal maltose transporter in Streptococcus mutans.
abstract: We report that a phosphoenolpyruvate-dependent phosphotransferase system, MalT, is the principal maltose transporter for Streptococcus mutans. MalT also contributes to maltotriose uptake. Since maltose and maltodextrins are products of starch degradation found in saliva, the ability to take up and ferment these carbohydrates may contribute to dental caries.
authors.affiliation: Microbiology, King's College London Dental Institute, Floor 28, Guy's Tower, King's College London, Guy's Campus, London SE1 9RT, United Kingdom.
authors.forename: Alexander J
authors.initials: AJ
authors.lastname: Webb
authors.forename: Karen A
authors.initials: KA
authors.lastname: Homer
authors.forename: Arthur H F
authors.initials: AH
authors.lastname: Hosie
mesh_terms: D001692:Biological Transport; D008320:Maltose / Q000378:metabolism*; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000502:physiology*; D013295:Streptococcus mutans / Q000201:enzymology*
chemical_list: D008320:Maltose; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System