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Updated: Oct 10, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

The kinetic mechanism of 5-enolpyruvylshikimate-3-phosphate synthase from a gram-positive pathogen Streptococcus

W Du1, N G Wallis, D J Payne

  • 1Anti-Infectives Research, SmithKline Beecham Pharmaceuticals, Collegeville, PA 19426, USA.

Journal of Enzyme Inhibition
|January 5, 2001
PubMed

Insights

Streptococcus pneumoniae EPSP synthase, a novel antibacterial target, exhibits unique kinetic inhibition patterns. Understanding its mechanism is key to developing new antibacterial agents.

Area of Science:

  • Biochemistry
  • Enzymology
  • Drug Discovery

Background:

  • Streptococcus pneumoniae 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase is a potential antibacterial target.
  • The enzyme catalyzes a crucial step in the shikimate pathway, essential for bacterial survival.

Purpose of the Study:

  • To elucidate the kinetic mechanism of S. pneumoniae EPSP synthase.
  • To investigate inhibition patterns by glyphosate (GLP) and reaction products.
  • To inform the design of novel antibacterial inhibitors.

Main Methods:

  • Steady-state kinetic studies.
  • Product inhibition assays.
  • Enzyme inhibition by glyphosate.

Main Results:

  • Glyphosate exhibits competitive inhibition with PEP and uncompetitive inhibition with S3P in the forward reaction.
  • EPSP acts as a competitive inhibitor against both PEP and S3P, suggesting a random sequential mechanism.
  • Inhibition patterns differ from other species, indicating unique enzymatic mechanisms.

Conclusions:

  • S. pneumoniae EPSP synthase displays distinct kinetic properties compared to orthologs.
  • These findings are critical for developing targeted antibacterial therapies against S. pneumoniae.
  • The enzyme's unique mechanism may be exploited for selective drug design.

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