Nature Communications (Jan 2017)

Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product

  • Jaeok Park,
  • Michal Zielinski,
  • Alexandr Magder,
  • Youla S. Tsantrizos,
  • Albert M. Berghuis

DOI
https://doi.org/10.1038/ncomms14132
Journal volume & issue
Vol. 8, no. 1
pp. 1 – 8

Abstract

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Farnesyl pyrophosphate (FPP) is a key building block for the synthesis of many lipids. Here the authors determine the crystal structure of farnesyl pyrophosphate synthase (FPPS) with its bound product and use kinetic measurements to show that FPP is an allosteric effector of the enzyme.