title: The characteristics of peptide uptake in Streptococcus faecalis: studies on the transport of natural peptides and antibacterial phosphonopeptides.
abstract: Transport of natural peptides and antibacterial phosphonopeptide analogues was studied in Streptococcus faecalis ATCC 9790. Competition studies, and the isolation of peptide-transport deficient mutants, indicate the presence of two peptide permeases. One is a high-rate system used by dipeptides, and to a lesser extent tripeptides; the other is a low-rate oligopeptide system. Following uptake, peptides are cleaved and their amino acid residues may undergo rapid exodus. Different strains of S. faecalis differ in their rates of peptide transport.
mesh_terms: D000409:Alanine / Q000031:analogs & derivatives / Q000378:metabolism; D000596:Amino Acids / Q000378:metabolism; D000615:Aminoethylphosphonic Acid / Q000378:metabolism; D004151:Dipeptides / Q000378:metabolism; D013293:Enterococcus faecalis / Q000378:metabolism*; D005450:Fluorescamine / Q000378:metabolism; D009842:Oligopeptides / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D004151:Dipeptides; D009842:Oligopeptides; C015670:2-aminooxypropionic acid; C004194:glycylsarcosine; D005450:Fluorescamine; D000615:Aminoethylphosphonic Acid; D000409:Alanine