Structure of limonene synthase, a simple model for terpenoid cyclase catalysis

Proc Natl Acad Sci U S A. 2007 Mar 27;104(13):5360-5. doi: 10.1073/pnas.0700915104. Epub 2007 Mar 19.


The crystal structure of (4S)-limonene synthase from Mentha spic ata, a metal ion-dependent monoterpene cyclase that catalyzes the coupled isomerization and cyclization of geranyl diphosphate, is reported at 2.7-A; resolution in two forms liganded to the substrate and intermediate analogs, 2-fluorogeranyl diphosphate and 2-fluorolinalyl diphosphate, respectively. The implications of these findings are described for domain interactions in the homodimer and for changes in diphosphate-metal ion coordination and substrate binding conformation in the course of the multistep reaction.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Catalysis
  • Crystallization
  • Crystallography, X-Ray
  • Intramolecular Lyases / chemistry*
  • Intramolecular Lyases / metabolism
  • Ions
  • Ligands
  • Mentha spicata / enzymology
  • Models, Chemical
  • Models, Molecular
  • Plant Proteins / chemistry
  • Protein Conformation
  • Protein Structure, Tertiary
  • Substrate Specificity
  • Terpenes / chemistry*


  • Ions
  • Ligands
  • Plant Proteins
  • Terpenes
  • Intramolecular Lyases
  • pinene cyclase I

Associated data

  • PDB/2ONG
  • PDB/2ONH