The effect of rutin on arginine kinase: inhibition kinetics and thermodynamics merging with docking simulation

Int J Biol Macromol. 2009 Mar 1;44(2):149-55. doi: 10.1016/j.ijbiomac.2008.11.007. Epub 2008 Nov 30.

Abstract

Arginine kinase (AK; EC 2.7.3.3) is a key enzyme in the cellular energy metabolism of insects. Screening on potential effective inhibitors of AK may provide a pathway for novel, environmentally friendly insecticides. The results in this study indicated that rutin, as a noncompetitive inhibitor, interacts with AK mainly by a hydrophobic force forming an intermolecular complex with AK, which is according to the thermodynamic parameters obtained. Using a flexible docking method (AutoDock) the interaction between rutin and AK were further analyzed, which suggested in order to screen effective inhibitors, flexible active sites of AK (Ser63, Gly64, Val65, Tyr68) should be taken in account.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arginine Kinase / antagonists & inhibitors*
  • Binding Sites
  • Computer Simulation*
  • Grasshoppers / enzymology
  • Hydrogen-Ion Concentration / drug effects
  • Kinetics
  • Models, Molecular*
  • Rutin / chemistry
  • Rutin / pharmacology*
  • Spectrometry, Fluorescence
  • Temperature
  • Thermodynamics

Substances

  • Rutin
  • Arginine Kinase