Inhibitory effect of phosphoenolpyruvate on glycolytic enzymes in Escherichia coli

Tadashi Ogawa, Hirotada Mori, Masaru Tomita, Masataka Yoshino

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36 Citations (Scopus)


For analyzing the control of energy metabolism in Escherichia coli, we carried out kinetic analyses of glycolytic enzymes purified from the overexpressing clones of E. coli K12 W3110 that were constructed with the vector pCA24N. Phosphoenolpyruvate (PEP) acted as an effective inhibitor of enzymes of the preparatory phase in glycolysis. Glucokinase was potently inhibited by PEP in a competitive manner with respect to ATP: the Ki value for PEP was 0.1 mM. PEP further inhibited phosphoglucoisomerase to a lesser extent, and phosphofructokinase A and aldolase A with 10-fold the Ki values of glucokinase and phosphoglucoisomerase. Glucose is incorporated into E. coli through two pathways: the PTS (PEP-dependent phosphotransferase system) and the glucokinase reaction. PEP, a potent inhibitor of E. coli glucokinase, unlike most eukaryotic hexokinases, can act as a signal molecule controlling glucose uptake and glycolytic flux in cells.

Original languageEnglish
Pages (from-to)159-163
Number of pages5
JournalResearch in Microbiology
Issue number2
Publication statusPublished - 2007 Mar


  • Escherichia coli
  • Glucokinase
  • Inhibition
  • Phosphoenolpyruvate
  • Phosphofructokinase
  • Phosphoglucoisomerase

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology


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