Evidence for the ionization steps in monoterpene cyclization reactions using 2-fluorogeranyl and 2-fluorolinalyl pyrophosphates as substrates.

  title={Evidence for the ionization steps in monoterpene cyclization reactions using 2-fluorogeranyl and 2-fluorolinalyl pyrophosphates as substrates.},
  author={Rodney B. Croteau},
  journal={Archives of biochemistry and biophysics},
  volume={251 2},
  • R. Croteau
  • Published 1 December 1986
  • Chemistry, Biology
  • Archives of biochemistry and biophysics

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

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

Terpene Cyclizations inside a Supramolecular Catalyst: Leaving-Group-Controlled Product Selectivity and Mechanistic Studies.

Control experiments demonstrate that a synergistic interplay between the supramolecular capsule and the acid traces is required for catalytic activity, and revealed that trace amounts of acid are required as cocatalyst.

Interception of the Enzymatic Conversion of Farnesyl Diphosphate to 5‐Epi‐Aristolochene by Using a Fluoro Substrate Analogue: 1‐Fluorogermacrene A from (2E,6Z)‐6‐Fluorofarnesyl Diphosphate

Steady‐state kinetic experiments with farnesyl PP and the 6‐fluoro analogue showed that the overall catalytic efficiencies (kcat/Km) are essentially the same for both substrates.

Terpene cyclization catalysed inside a self-assembled cavity.

Evidence indicates that the direct isomerization of a geranyl cation to the cisoid isomer, which so far was considered unlikely, is feasible and the first example of a successful THT cyclization inside a supramolecular structure is reported.

A 1,6-ring closure mechanism for (+)-δ-cadinene synthase?

The results reported here do not unambiguously rule in favor of 1,6- or 1,10-cyclization, but demonstrate the mechanistic versatility inherent to DCS and highlight the possible existence of multiple mechanistic pathways.



Mechanism of the pyrophosphate migration in the enzymatic cyclization of geranyl and linalyl pyrophosphates to (+)- and (-)-bornyl pyrophosphates.

The absence of P alpha-P beta interchange and the complete lack of positional 18O isotope exchange of the pyrophosphate moiety are compatible with tight ion pairing of intermediates in the coupled isomerization-cyclization of geranyl pyroph phosphate and establish a remarkably tight restriction on the motion of the transiently generated pyphosphate anion with respect to its cationic terpenyl reaction partner.

Farnesyl pyrophosphate synthetase. Mechanistic studies of the 1'-4 coupling reaction with 2-fluorogeranyl pyrophosphate.

These data are interpreted in terms of an ionization-condensation-elimination mechanism for the 1'-4 coupling reaction, which shows 2-fluorogeranyl pyrophosphate is a competitive inhibitor against geranyl pyphosphate.