Using Terpene Synthase Plasticity in Catalysis: On the Enzymatic Conversion of Synthetic Farnesyl Diphosphate Analogues

Chemistry. 2021 Nov 11;27(63):15644-15649. doi: 10.1002/chem.202103049. Epub 2021 Sep 29.

Abstract

Four synthetic farnesyl diphosphate analogues were enzymatically converted with three bacterial sesquiterpene synthases, including β-himachalene synthase (HcS) and (Z)-γ-bisabolene synthase (BbS) from Cryptosporangium arvum, and germacrene A synthase (SmTS6) from Streptomyces mobaraensis. These enzyme reactions not only yielded several previously unknown compounds, showing that this approach opened the door to a new chemical space, but substrates with blocked or altered reactivities also gave interesting insights into the cyclisation mechanisms and the potential to catalyse reactions with different initial cyclisation modes.

Keywords: biosynthesis; configuration determination; enzymes; substrate analogues; terpenoids.

MeSH terms

  • Actinobacteria
  • Alkyl and Aryl Transferases*
  • Catalysis
  • Polyisoprenyl Phosphates
  • Sesquiterpenes*
  • Streptomyces

Substances

  • Polyisoprenyl Phosphates
  • Sesquiterpenes
  • farnesyl pyrophosphate
  • Alkyl and Aryl Transferases
  • terpene synthase

Supplementary concepts

  • Cryptosporangium arvum
  • Streptomyces mobaraensis