Mechanism of Interaction of Phospholipase A2 with Phospholipid Substrates and Activators

  • Edward A. Dennis
  • Andreas Plückthun
Part of the NATO ASI Series book series (NSSA, volume 116)


Phospholipase A2 is one of the smallest and simplest enzymes of lipid metabolism (1). Over the last several years, our laboratory has been focusing on the mechanism by which it interacts with phospholipid in the lipid-water interface and achieves an extraordinary increase in activity over manomerically dispersed substrate. This increase is observed on both micelles of synthetic short chain phospholipid substrates and on mixed micelles with detergents such as Triton X-100. This requirement for an interface for maximal activity has puzzled enzymologists for years.


Immobilize Enzyme Mixed Micelle Soluble Enzyme Fatty Acid Product Cobra Venom 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Edward A. Dennis
    • 1
  • Andreas Plückthun
    • 1
  1. 1.Department of ChemistryUniversity of California at San DiegoLa JollaUSA

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