Escherichia coli phosphoenolpyruvate dependent phosphotransferase system. Copurification of HPr and alpha 1-6 glucan

Biochemistry. 1979 Jul 10;18(14):2990-6. doi: 10.1021/bi00581a013.

Abstract

A rapid, high-yield procedure has been developed for the purification of HPr from the Escherichia coli phosphoenolpyruvate dependent phosphotransferase system. During this procedure, the protein copurifies with a 2500-dalton homopolysaccharide which we have identified as alpha 1-6 glucan. The results of steady-state kinetic measurements of the phosphotransferase activity demonstrate that the polysaccharide works as an activator of the phosphotransferase system probably at the level of the HPr:P-E1 complex or the P-HPr:E11 complex.

MeSH terms

  • Bacterial Proteins / isolation & purification*
  • Carbohydrates / analysis
  • Chemical Phenomena
  • Chemistry
  • Escherichia coli / enzymology*
  • Glucans / isolation & purification*
  • Magnetic Resonance Spectroscopy
  • Models, Biological
  • Molecular Conformation
  • Molecular Weight
  • Phosphates / analysis
  • Phosphoenolpyruvate / metabolism*
  • Phosphotransferases / metabolism*
  • Polysaccharides, Bacterial / analysis*

Substances

  • Bacterial Proteins
  • Carbohydrates
  • Glucans
  • Phosphates
  • Polysaccharides, Bacterial
  • Phosphoenolpyruvate
  • Phosphotransferases