Inhibitors of the herbicidal target IspD: Allosteric site binding

Link:
Autor/in:
Erscheinungsjahr:
2011
Medientyp:
Text
Schlagworte:
  • Phosphates
  • Terpenes
  • Phosphate MEP
  • Rubber
  • Diphosphates
  • protein-ligand interactions
  • allosteric binding
  • structure-activity relationship
  • medicinal chemistry
  • herbicides
  • Phosphates
  • Terpenes
  • Phosphate MEP
  • Rubber
  • Diphosphates
Beschreibung:
  • The pick of the pockets : The first inhibitors for IspD, an enzyme from the non‐mevalonate pathway of isoprenoid biosynthesis, are described. High‐throughput‐screening revealed a hit with an IC50 value of 140 nM . Co‐crystal structure analyses of the binding mode in the newly formed allosteric pocket (see structure, red ball: water O atom), lead to the synthesis of a set of 17 derivatives which were tested to optimize the herbicidal activity.
Lizenz:
  • info:eu-repo/semantics/restrictedAccess
Quellsystem:
Forschungsinformationssystem der UHH

Interne Metadaten
Quelldatensatz
oai:www.edit.fis.uni-hamburg.de:publications/711b1ad9-cccf-4fee-8492-1d72e6d2e812