Resolution of the phosphoenolpyruvate: fructose phosphotransferase system of Escherichia coli into two components: enzyme IIfructose and fructose-induced HPr-like protein (FPr)

Can J Biochem. 1980 Oct;58(10):1144-6. doi: 10.1139/o80-153.


A protein that substitutes for histidine-containing protein (HPr) in the phosphoenolpyruvate, fructose phosphotransferase system has been found in Escherichia coli grown on fructose. The impure preparation of the fructose-induced HPr-like protein (FPr) appears to be an extrinsic membrane protein which differs from HPr on the basis of its apparent molecular weight (45 000 vs. 9600, respectively), its affinity for DEAE-cellulose and its ability to promote sugar phosphorylation which is specific for fructose, rather than for glucose.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Carrier Proteins / isolation & purification*
  • Carrier Proteins / metabolism
  • Enzyme Induction
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins*
  • Fructose / pharmacology
  • Intracellular Signaling Peptides and Proteins
  • Kinetics
  • Mutation
  • Phenotype
  • Phosphoenolpyruvate Sugar Phosphotransferase System / isolation & purification*
  • Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism
  • Phosphorylation
  • Protein Kinases
  • Substrate Specificity
  • Sugar Phosphates / biosynthesis


  • Bacterial Proteins
  • Carrier Proteins
  • Escherichia coli Proteins
  • Intracellular Signaling Peptides and Proteins
  • Sugar Phosphates
  • fructose-induced HPr-like protein, bacteria
  • Fructose
  • Protein Kinases
  • fruB protein, E coli
  • Phosphoenolpyruvate Sugar Phosphotransferase System