Sugar transport by the bacterial phosphotransferase system. Primary structure and active site of a general phosphocarrier protein (HPr) from Salmonella typhimurium.

@article{Weigel1982SugarTB,
  title={Sugar transport by the bacterial phosphotransferase system. Primary structure and active site of a general phosphocarrier protein (HPr) from Salmonella typhimurium.},
  author={NetworksR. S. Weigel and Dennis A. Powers and Saul Roseman},
  journal={The Journal of biological chemistry},
  year={1982},
  volume={257 23},
  pages={14499-509}
}
The general histidine-containing phosphocarrier protein (HPr) of the Salmonella phosphotransferase system is required for the phosphorylation of all sugar substrates by this system. The complete amino acid sequence of HPr, consisting of 84 amino acid residues, has been established. The sequence was determined by cleaving the protein with cyanogen bromide, trypsin, and with a protease from Staphylococcus aureus, followed by isolation and amino acid sequence determination of the resulting… CONTINUE READING

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