The molecular mechanism of bee venom phospholipase A2 inactivation by bolinaquinone

Chembiochem. 2006 Jun;7(6):971-80. doi: 10.1002/cbic.200500454.

Abstract

The molecular basis of the inactivation of bee venom PLA2 by the marine natural product bolinaquinone (BLQ) was studied by several spectral techniques (CD, fluorescence, and NMR spectroscopy, mass spectrometry), biomimetic reactions, and molecular modeling. Our data suggest competitive inhibition based on a BLQ-PLA2 noncovalent molecular recognition. However, BLQ is also able to react selectively with Lys133 through conjugate addition followed by a beta elimination. The biological implications of both the covalent and noncovalent molecular events are discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bee Venoms / enzymology*
  • Binding Sites
  • Chromatography, High Pressure Liquid
  • Circular Dichroism
  • Fluorescence
  • Kinetics
  • Models, Molecular
  • Molecular Structure
  • Phospholipases A / antagonists & inhibitors
  • Phospholipases A / chemistry*
  • Phospholipases A / metabolism
  • Phospholipases A2
  • Protein Binding
  • Sesquiterpenes / chemistry*
  • Sesquiterpenes / pharmacology
  • Spectrometry, Mass, Electrospray Ionization

Substances

  • Bee Venoms
  • Sesquiterpenes
  • bolinaquinone
  • Phospholipases A
  • Phospholipases A2