title: Synthesis of heterocyclic terpenoids by promiscuous squalene-hopene cyclases.
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.
authors: Institute of Technical Biochemistry, Universität Stuttgart, Allmandring 31, 70569 Stuttgart, Germany.
authors: Miriam
authors: M
authors: Seitz
authors: Per-Olof
authors: PO
authors: Syrén
authors: Lisa
authors: L
authors: Steiner
authors: Janosch
authors: J
authors: Klebensberger
authors: Bettina M
authors: BM
authors: Nestl
authors: Bernhard
authors: B
authors: Hauer
mesh_terms: D056450:Alicyclobacillus / Q000201:enzymology* / Q000378:metabolism; D003500:Cyclization; D019751:Intramolecular Transferases / Q000378:metabolism*; D008958:Models, Molecular; D013379:Substrate Specificity; D013729:Terpenes / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D013729:Terpenes; D019751:Intramolecular Transferases; C066630:squalene-hopene cyclase