3790-71-4

Usage

InChI:InChI=1/C15H26O/c1-13(2)7-5-8-14(3)9-6-10-15(4)11-12-16/h7,9,11,16H,5-6,8,10,12H2,1-4H3/b14-9+,15-11-

Upstream product

• 59905-15-6 dehydronerolidol 
• 40716-66-3 (E)-3,7,11-trimethyl-1,6,10-dodecatrien-3-ol 
• 50-00-0 formaldehyd 
• 3796-70-1 trans geranyl acetone 
• 1779-49-3 Methyltriphenylphosphonium bromide 
• 33776-65-7 ethyl (2Z/E,6E)-3,7,11-trimethyldodeca-2,6,10-trienoate 
• 358-71-4 isopentyl pyrophosphate 
• 763-10-0 geranyl diphosphate 
• 19317-11-4 farnesal 
• 72019-02-4 (6E)-3,7,11-trimethyldodeca-2,6,10-trienal 
• 358-72-5 dimethylallyl diphosphate 
• 226090-90-0 (6E)-farnesyl acetate 
• 108-24-7 acetic anhydride 
• 4602-84-0 farnesol 

Downstream Products

• 17627-44-0 α-bisabolene 
• 495-62-5 γ-bisabolene 
• 468-68-8 epi-drimenol 
• 28413-58-3 cis, trans-farnesyl phenyl sulfide 
• 40716-66-3 (E)-3,7,11-trimethyl-1,6,10-dodecatrien-3-ol 
• 60441-28-3 cis, trans-germacradiene 
• 74986-29-1 10,11-epoxy-cis, trans-farnesyl phenyl sulfide 
• 104764-30-9 (1S,2R)-2-((E)-1,5-Dimethyl-hexa-1,4-dienyl)-5,5-dimethyl-cyclohexanol 
• 6750-34-1 (3R,7R)-hexahydrofarnesol 
• 203057-25-4 trans-muurola-4⁽¹⁴⁾,5-diene 
• 92692-39-2 (1R,4R,4aS,8aR)-4,7-dimethyl-1-(prop-1-en-2-yl)-1,2,3,4,4a,5,6,8a-octahydronaphthalene 
• 196402-66-1 β-sesquiphellandrene 
• 1252598-69-8 C₂₈H₄₂O₄ 
• 469-61-4 (+/-)-cedrene 

Relevant academic research and scientific papers

METHOD FOR PRODUCING CARBOXYLIC ACID PRENYL AND PRENOL

PROBLEM TO BE SOLVED: To provide a method for producing carboxylic acid prenyls and prenols in high yields and in an industrial and economical advantageous manner. SOLUTION: A production method includes reacting a prenyl amine represented by formula (1), in the presence of a halide, with a carboxylic acid anhydride represented by formula (2), to produce a carboxylic acid prenyl represented by formula (3), and further subjecting the carboxylic acid prenyl to solvolysis, to obtain a prenol represented by formula (6). SELECTED DRAWING: None COPYRIGHT: (C)2020,JPOandINPIT

Structure-Function Studies of Artemisia tridentata Farnesyl Diphosphate Synthase and Chrysanthemyl Diphosphate Synthase by Site-Directed Mutagenesis and Morphogenesis

The amino acid sequences of farnesyl diphosphate synthase (FPPase) and chrysanthemyl diphosphate synthase (CPPase) from Artemisia tridentata ssp. Spiciformis, minus their chloroplast targeting regions, are 71% identical and 90% similar. FPPase efficiently and selectively synthesizes the "regular" sesquiterpenoid farnesyl diphosphate (FPP) by coupling isopentenyl diphosphate (IPP) to dimethylallyl diphosphate (DMAPP) and then to geranyl diphosphate (GPP). In contrast, CPPase is an inefficient promiscuous enzyme, which synthesizes the "irregular" monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP. A. tridentata FPPase and CPPase belong to the chain elongation protein family (PF00348), a subgroup of the terpenoid synthase superfamily (CL0613) whose members have a characteristic α terpene synthase α-helical fold. The active sites of A. tridentata FPPase and CPPase are located within a six-helix bundle containing amino acids 53 to 241. The two enzymes were metamorphosed into one another by sequentially replacing the loops and helices of the six-helix bundle from enzyme with those from the other. Chain elongation was the dominant activity during the N-terminal to C-terminal metamorphosis of FPPase to CPPase, with product selectivity gradually switching from FPP to GPP, until replacement of the final α-helix, whereupon cyclopropanation and branching activity competed with chain elongation. During the corresponding metamorphosis of CPPase to FPPase, cyclopropanation and branching activities were lost upon replacement of the first helix in the six-helix bundle. Mutations of active site residues in CPPase to the corresponding amino acids in FPPase enhanced chain-elongation activity, while similar mutations in the active site of FPPase failed to significantly promote formation of significant amounts of irregular monoterpenes. Our results indicate that CPPase, a promiscuous enzyme, is more plastic toward acquiring new activities, whereas FPPase is more resistant. Mutations of residues outside of the α terpene synthase fold are important for acquisition of FPPase activity for synthesis of CPP, LPP, and MPP.

MANUFACTURING METHOD OF CARBOXYLIC ACID PRENYL AND PRENOL USING OXOVANADIUM COMPLEX

PROBLEM TO BE SOLVED: To provide an industrially and economically advantageous manufacturing method of carboxylic acid prenyl and prenol in a high yield under a mild condition. SOLUTION: In a manufacturing method, allyl alcohol represented by the formula (1) is reacted with carboxylic acid anhydride represented by the formula (2) in a presence of an oxovanadium complex prepared by reacting trialkoxy oxovanadium and a pyridinecarboxylic acid derivative, thereby obtaining allyl ester represented by the formula (3). Further, carboxylic acid prenyl is subjected to solvolysis, thereby obtaining prenol represented by the formula (4). SELECTED DRAWING: None COPYRIGHT: (C)2017,JPO&INPIT

MANUFACTURING METHOD OF PRENYL CARBOXYLATES AND PRENOLS USING BIS(β-DIKETONATO)DIOXO MOLYBDENUM COMPLEX

PROBLEM TO BE SOLVED: To provide an environmental friendly, simple, safe and inexpensive manufacturing method of prenyl carboxylates and prenols which are useful as raw materials or synthetic intermediates of pharmaceuticals, agricultural chemicals, aromatics or the like. SOLUTION: There are provided a manufacturing method of prenyl carboxylates represented by the formula (3) by reacting allyl alcohols represents by the formula (1) with carboxylic acid anhydride represented by the formula (2) in a presence of bis(β-diketonato)dioxo molybdenum complex and further a manufacturing method of prenols represented by the formula (4) by solvolysis of prenyl carboxylates represented by the formula (3) with methanol or the like in a presence of a catalyst such as potassium carbonate. SELECTED DRAWING: None COPYRIGHT: (C)2017,JPO&INPIT

PRODUCTION OF FARNESOL

The present invention relates to an improved way for the production of farnesol.

METHOD FOR PRODUCING PRENYL ESTERS AND PRENOLS

PROBLEM TO BE SOLVED: To provide an industrially and economically advantageous method for geometrically selectively producing prenol under a mild condition. SOLUTION: Provided is a method for producing prenyl ester (3) in which allyl alcohol (1) is reacted with vinyl ester (2) under the presence of an oxovanadium complex and a hydrolytic enzyme. Further provided is a method for producing prenol (4) by hydrolyzing prenyl ester (3). SELECTED DRAWING: None COPYRIGHT: (C)2017,JPOandINPIT

(2E, 6E) enriching [...] -

PROBLEM TO BE SOLVED: To provide a method for producing (2E, 6E)-farnesal useful as an intermediate for the production of a polyisoprenoid derivative useful as an anticancer agent.SOLUTION: The method for producing (2E, 6E)-farnesal includes heating (2Z, 6E)-farnesal in the presence of a piperidin-1-oxyl compound represented by formula (1) [wherein Ris a hydrogen atom; Ris a hydrogen atom, cyano, carboxy, isothiocyanato, maleimide, phosphate group, -OR' group or -NHR group (wherein R' is a hydrogen atom, 1-4C alkyl, acyl or 1-4C alkanesulfonyl; R is a hydrogen atom, acetyl or haloacetyl); or Rand Rtogether form an oxo group].

Method for Converting Farnesol to Nerolidol in the Presence of Alpha-Bisabolol

A method for converting farnesol to nerolidol in the presence of alpha-bisabolol including providing or preparing a mixture of alpha-bisabolol, farnesol, and one or more catalysts for selective isomerization of farnesol to nerolidol in the presence of alpha-bisabolol, and converting at least a portion of the farnesol to nerolidol.

Substrate specificities of E- and Z-farnesyl diphosphate synthases with substrate analogs

Prenyltransferases catalyzes the basic isoprenoid chain elongation to produce prenyl diphosphates, which led to upward of 30,000 diverse isoprenoids as steroids, carotenoids, natural rubbers, and prenyl proteins. Here, we determined the reactivities of E- and Z-farnesyl diphosphate synthases (E- and Z-FPP synthases) isolated from Bacillus stearothermophilus and Thermobifida fusca, respectively. For this purpose we use the synthetic substrate analogs, 8-tetrahydropyran-2-yloxy-, 8-hydroxy- and 8-acetoxygeranyl diphosphates. Z-FPP synthase catalyzed the reaction between 8-hydroxygeranyl diphosphate (HOGPP) and isopentenyl diphosphate (IPP), which produced (2Z)-12-hydroxyfarnesyl diphosphate (yield: 16.7%) and (2Z, 6Z)-16-hydroxygeranylgeranyl diphosphate (yield: 6.6%). Neither E- nor Z-farnesyl diphosphate synthases detectably catalyzed reactions between 8-tetrahydropyran-2-yloxygeranyl diphosphate (8-THPOGPP) and IPP. However, a mutated E-FPP synthase (Y81S), did catalyze this reaction, producing 12-tetrahydropyran-2-yloxyfarnesyl diphosphate (12-THPOFPP) with a yield of 12.3%. Wild-type E-FPP synthase catalyzed the reaction of 8-acetoxygeranyl diphosphate (8-AcOGPP) with IPP, which produced 12-acetoxyfarnesyl diphosphate (12-AcOFPP) (yield, 21.8%). Mutant E-FPP synthase catalyzed the reaction between 8-AcOGPP with IPP, producing 12-AcOFPP and 16-acetoxygeranylgeranyl diphosphate (16-AcOGGPP) with respective yields of 55.3% and 1.7%. We believe our results contribute to a better understanding of the catalytic properties of these key enzymes and illustrate their use in the stereo-specific syntheses of compounds that may have significant biotechnological and medical applications.

Structural elucidation of cisoid and transoid cyclization pathways of a sesquiterpene synthase using 2-fluorofarnesyl diphosphates

Sesquiterpene skeletal complexity in nature originates from the enzyme-catalyzed ionization of (trans,trans)-farnesyl diphosphate (FPP) (1a) and subsequent cyclization along either 2,3-transoid or 2,3-cisoid farnesyl cation pathways. Tobacco 5-epi-aristolochene synthase (TEAS), a transoid synthase, produces cisoid products as a component of its minor product spectrum. To investigate the cryptic cisoid cyclization pathway in TEAS, we employed (cis,trans)-FPP (1b) as an alternative substrate. Strikingly, TEAS was catalytically robust in the enzymatic conversion of (cis,trans)-FPP (1b) to exclusively (?99.5%) cisoid products. Further, crystallographic characterization of wild-type TEAS and a catalytically promiscuous mutant (M4 TEAS) with 2-fluoro analogues of both all-trans FPP (1a) and (cis,trans)-FPP (1b) revealed binding modes consistent with preorganization of the farnesyl chain. These results provide a structural glimpse into both cisoid and transoid cyclization pathways efficiently templated by a single enzyme active site, consistent with the recently elucidated stereochemistry of the cisoid products. Further, computational studies using density functional theory calculations reveal concerted, highly asynchronous cyclization pathways leading to the major cisoid cyclization products. The implications of these discoveries for expanded sesquiterpene diversity in nature are discussed.