1,3-Phenylene bis(ketoacid) derivatives as inhibitors of Escherichia coli dihydrodipicolinate synthase

Bioorg Med Chem. 2012 Apr 1;20(7):2419-26. doi: 10.1016/j.bmc.2012.01.045. Epub 2012 Feb 10.

Abstract

Dihydrodipicolinate synthase is a key enzyme in the lysine biosynthesis pathway that catalyzes the condensation of pyruvate and aspartate semi-aldehyde. A series of phenolic ketoacid derivatives that mimic the proposed enzymatic intermediate were designed as potential inhibitors of this enzyme and were synthesized from simple precursors. The ketoacid derivatives were shown to act as slow and slow-tight binding inhibitors. Mass spectrometric experiments provided further evidence to support the proposed model of inhibition, demonstrating either an encounter complex or a condensation product for the slow and slow-tight binding inhibitors, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry*
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins / antagonists & inhibitors*
  • Escherichia coli Proteins / metabolism
  • Hydro-Lyases / antagonists & inhibitors*
  • Hydro-Lyases / metabolism
  • Keto Acids / chemical synthesis
  • Keto Acids / chemistry*
  • Kinetics
  • Mass Spectrometry

Substances

  • Enzyme Inhibitors
  • Escherichia coli Proteins
  • Keto Acids
  • Hydro-Lyases
  • 4-hydroxy-tetrahydrodipicolinate synthase