The intramembrane topography of the mannitol-specific enzyme II of the Escherichia coli phosphotransferase system.
The D-mannitol-specific Enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli is an integral cytoplasmic membrane protein responsible for concomitant transport and phosphorylation of this hexitol. We have investigated the intramembrane topography of this enzyme/permease using proteases, membrane-impermeable reagents, and antibodies against the purified protein. The results of these experiments suggest that this protein spans the membrane in a single orientation with a sizeable proportion of its mass extending into the cytoplasm, but with little of the polypeptide exposed at the outside surface of the membrane. Such an orientation is consistent with the reception and transport roles of the mannitol Enzyme II in E. coli.
D002462:Cell Membrane / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D007700:Kinetics; D008970:Molecular Weight; D009004:Monosaccharide Transport Proteins; D010446:Peptide Fragments / Q000032:analysis; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism*; D013104:Spheroplasts / Q000201:enzymology
D029968:Escherichia coli Proteins; D009004:Monosaccharide Transport Proteins; D010446:Peptide Fragments; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C022358:mannitol PTS permease, E coli