18794-84-8Relevant articles and documents
Brieger
, p. 3720 (1967)
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White,J.D.,Gupta,D.N.
, p. 3331 - 3339 (1969)
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Ohloff,G. et al.
, p. 561 - 570 (1967)
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Syntheses of All-trans Acyclic Isoprenoid Pheromone Components
Baeckstroem, Peter,Li, Lanna
, p. 6533 - 6538 (1991)
All-trans acyclic isoprenoid skeletons were made through a two-step iterative sequence.The method involves the Claisen rearrangement of allyl vinyl ethers formed from allylic alcohols and the dimethyl acetal of methyl isopropenyl ketone, followed by LiAlH4 reduction of the α,β-unsaturated ketone formed by rearrangement.The α,β-unsaturated ketone was also transformed to the 2-methyl-1-propenyl group by using a one-pot deoxygenation reaction for the synthesis of (E)-β-farnesene, (E)-β-springene and dendrolasin.
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Mimura,T. et al.
, p. 1361 - 1364 (1979)
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Andersen,Syrdal
, p. 2455 (1972)
Enantioselective Conversion of Oligoprenol Derivatives to Macrocycles in the Germacrene, Cembrene, and 18-Membered Cyclic Sesterterpene Series
Reddy, D. Srinivas,Corey
supporting information, p. 16909 - 16913 (2018/12/14)
A new enantio-and diastereoselective process has been developed for the efficient conversion of farnesol and other oligoprenyl alcohols to chiral 10-, 14-, and 18-membered cyclization products, including germacrenol, (+)-costunolide, 3-β-elemol, and epi-mukulol. The key cyclization reaction utilizes ω-bromo aldehyde substrates, a chiral ligand, and indium powder as the reagent at -78 °C and generates 10-, 14-, and 18-membered cyclic products in 70-74% yield and 94-95% ee.
Mechanism-Based Post-Translational Modification and Inactivation in Terpene Synthases
Kersten, Roland D.,Diedrich, Jolene K.,Yates, John R.,Noel, Joseph P.
, p. 2501 - 2511 (2015/12/01)
Terpenes are ubiquitous natural chemicals with diverse biological functions spanning all three domains of life. In specialized metabolism, the active sites of terpene synthases (TPSs) evolve in shape and reactivity to direct the biosynthesis of a myriad of chemotypes for organismal fitness. As most terpene biosynthesis mechanistically involves highly reactive carbocationic intermediates, the protein surfaces catalyzing these cascade reactions possess reactive regions possibly prone to premature carbocation capture and potentially enzyme inactivation. Here, we show using proteomic and X-ray crystallographic analyses that cationic intermediates undergo capture by conserved active site residues leading to inhibitory self-alkylation. Moreover, the level of cation-mediated inactivation increases with mutation of the active site, upon changes in the size and structure of isoprenoid diphosphate substrates, and alongside increases in reaction temperatures. TPSs that individually synthesize multiple products are less prone to self-alkylation then TPSs possessing relatively high product specificity. In total, the results presented suggest that mechanism-based alkylation represents an overlooked mechanistic pressure during the evolution of cation-derived terpene biosynthesis.
