Synthesis of heterocyclic terpenoids by promiscuous squalene-hopene cyclases

Chembiochem. 2013 Mar 4;14(4):436-9. doi: 10.1002/cbic.201300018. Epub 2013 Feb 18.

Abstract

PROMISCUOUS ENZYMES: The substrate promiscuity of squalene-hopene cyclases has been explored and applied in the enzyme-catalyzed synthesis of heterocyclic terpenoids. Features of this work include cyclization reactions without pyrophosphate activation, and stereospecific ring closure of substrates of varying chain length and terminal nucleophile. This provides a biocatalytic alternative to traditional chemical catalysts.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alicyclobacillus / enzymology*
  • Alicyclobacillus / metabolism
  • Cyclization
  • Intramolecular Transferases / metabolism*
  • Models, Molecular
  • Substrate Specificity
  • Terpenes / chemistry*
  • Terpenes / metabolism*

Substances

  • Terpenes
  • Intramolecular Transferases
  • squalene-hopene cyclase