76947-02-9Relevant articles and documents
Methyl-Shifted Farnesyldiphosphate Derivatives Are Substrates for Sesquiterpene Cyclases
Harms, Vanessa,Schr?der, Benjamin,Oberhauser, Clara,Tran, Cong Duc,Winkler, Sven,Dr?ger, Gerald,Kirschning, Andreas
supporting information, p. 4360 - 4365 (2020/06/08)
New sesquiterpene backbones are accessible after biotransformation of presilphiperfolan-8β-ol synthase (BcBOT2), a fungal sesquiterpene synthase, with non-natural farnesyldiphosphates in which methyl groups are shifted by one position toward the diphosphate terminus. One of the macrocycles formed, a new germacrene A derivative, undergoes a Cope rearrangement to iso-β-elemene. Three of the new terpenoids show olfactoric properties that range from an intense peppery note to a citrus, ozone-like, and fruity scent.
Characterization of the first naturally thermostable terpene synthases and development of strategies to improve thermostability in this family of enzymes
Styles, Matthew Q.,Nesbitt, Edward A.,Marr, Scott,Hutchby, Marc,Leak, David J.
, p. 1700 - 1711 (2017/06/08)
The terpenoid family of natural products is being targeted for heterologous microbial production as a cheaper and more reliable alternative to extraction from plants. The key enzyme responsible for diversification of terpene structure is the class-I terpene synthase (TS), and these often require engineering to improve properties such as thermostability, robustness and catalytic activity before they are suitable for industrial use. Improving thermostability typically relies on screening a large number of mutants, as there are no naturally thermostable TSs described upon which to base rational design decisions. We have characterized the first examples of natural TSs exhibiting thermostability, which catalyse the formation of the sesquiterpene τ-muurolol at temperatures up to 78 °C. We also report an enzyme with a kcat value of 0.95 s?1 at 65 °C, the highest kcat recorded for a bacterial sesquiterpene synthase. In turn, these thermostable enzymes were used as a model to inform the rational engineering of another TS, with the same specificity but low sequence identity to the model. The newly engineered variant displayed increased thermostability and turnover. Given the high structural homology of the class-I TS domain, this approach could be generally applicable to improving the properties of other enzymes in this class. Database: Model data are available in the PMDB database under the accession number PM0080780.
IspG converts an epoxide substrate analogue to (E)-4-hydroxy-3-methylbut-2- enyl diphosphate: Implications for IspG catalysis in isoprenoid biosynthesis
Nyland II, Rodney L.,Xiao, Youli,Liu, Pinghua,Freel Meyers, Caren L.
supporting information; experimental part, p. 17734 - 17735 (2010/04/01)
(Chemical Equation Presented) IspG is an intriguing enzyme in bacteria, parasite, and plant isoprenoid biosynthesis, and its catalytic mechanism remains elusive. We report here the synthesis of (2R,3R)-4-hydroxy-3-methyl-2,3- epoxybutanyl diphosphate (Epoxy-HMBPP), a proposed intermediate in one of the frequently cited mechanistic models. We have also demonstrated that this epoxide analogue is a catalytically competent IspG substrate. This study represents the first mechanistic study of this important enzyme.
