Inhibitory effect of phosphoenolpyruvate on glycolytic enzymes in Escherichia coli

Tadashi Ogawa, Hirotada Mori, Masaru Tomita, Masataka Yoshino

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

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
Volume158
Issue number2
DOIs
Publication statusPublished - 2007 Mar

Fingerprint

Phosphoenolpyruvate
Glucokinase
Escherichia coli
Enzymes
Glucose
Escherichia coli K12
Phosphofructokinases
Fructose-Bisphosphate Aldolase
Hexokinase
Enzyme Inhibitors
Glycolysis
Energy Metabolism
Phosphotransferases
Clone Cells
Adenosine Triphosphate

Keywords

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

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Microbiology

Cite this

Inhibitory effect of phosphoenolpyruvate on glycolytic enzymes in Escherichia coli. / Ogawa, Tadashi; Mori, Hirotada; Tomita, Masaru; Yoshino, Masataka.

In: Research in Microbiology, Vol. 158, No. 2, 03.2007, p. 159-163.

Research output: Contribution to journalArticle

Ogawa, Tadashi ; Mori, Hirotada ; Tomita, Masaru ; Yoshino, Masataka. / Inhibitory effect of phosphoenolpyruvate on glycolytic enzymes in Escherichia coli. In: Research in Microbiology. 2007 ; Vol. 158, No. 2. pp. 159-163.
@article{4365ebd276e8451199cb0aa93a072c1f,
title = "Inhibitory effect of phosphoenolpyruvate on glycolytic enzymes in Escherichia coli",
abstract = "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.",
keywords = "Escherichia coli, Glucokinase, Inhibition, Phosphoenolpyruvate, Phosphofructokinase, Phosphoglucoisomerase",
author = "Tadashi Ogawa and Hirotada Mori and Masaru Tomita and Masataka Yoshino",
year = "2007",
month = "3",
doi = "10.1016/j.resmic.2006.11.003",
language = "English",
volume = "158",
pages = "159--163",
journal = "Research in Microbiology",
issn = "0923-2508",
publisher = "Elsevier Masson SAS",
number = "2",

}

TY - JOUR

T1 - Inhibitory effect of phosphoenolpyruvate on glycolytic enzymes in Escherichia coli

AU - Ogawa, Tadashi

AU - Mori, Hirotada

AU - Tomita, Masaru

AU - Yoshino, Masataka

PY - 2007/3

Y1 - 2007/3

N2 - 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.

AB - 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.

KW - Escherichia coli

KW - Glucokinase

KW - Inhibition

KW - Phosphoenolpyruvate

KW - Phosphofructokinase

KW - Phosphoglucoisomerase

UR - http://www.scopus.com/inward/record.url?scp=33847365007&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33847365007&partnerID=8YFLogxK

U2 - 10.1016/j.resmic.2006.11.003

DO - 10.1016/j.resmic.2006.11.003

M3 - Article

C2 - 17307338

AN - SCOPUS:33847365007

VL - 158

SP - 159

EP - 163

JO - Research in Microbiology

JF - Research in Microbiology

SN - 0923-2508

IS - 2

ER -