13920-11-1

Basic information

• Product Name: Geranylcitral
• CAS NO: 13920-11-1
• Molecular Weight: 288.473
• Mol File: 13920-11-1.mol

Chemical Properties

• CAS DataBase Reference: Geranylcitral(CAS DataBase Reference)
• NIST Chemistry Reference: Geranylcitral(13920-11-1)
• EPA Substance Registry System: Geranylcitral(13920-11-1)

Safety Data

• Hazardous Substances Data: 13920-11-1(Hazardous Substances Data)

Upstream product

• 51921-98-3 (4E,8E)-ethyl 2-acetyl-5,9,13-trimethyltetradeca-4,8,12-trienoate 
• 24163-93-7 farnesyl bromide 
• 106-28-5 Farnesol 
• 24035-35-6 (2E,6E,10E)-3,7,11,15-tetramethyl-hexadeca-2,6,10,14-tetraenoic acid ethyl ester 
• 1117-52-8 6,10,14-trimethyl-5,9,13-pentadecatriene-2-on 
• 24034-73-9 Geranylgeraniol 
• 42207-88-5 (2E,6E,10E)-methyl 3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenoate 

Downstream Products

• 32304-16-8 (all-E)-3,7,11,15,19,23,27-Heptamethyloctacosa-2,6,10,14,18,22,26-heptaen-1-ol 
• 180627-83-2 N-((2E,6E,10E)-3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylidene)cyclohexylamine 
• 24286-51-9 (+/-)-Casbene 
• 13920-14-4 phytofluene 

Relevant articles and documents

Mimicking Halimane Synthases: Monitoring a Cascade of Cyclizations and Rearrangements from Epoxypolyprenes

We have developed and rationalized a biomimetic transformation mimicking halimane synthases based on a Lewis acid-catalyzed cascade of cyclizations and rearrangements of epoxypolyprenes. Two rings, three stereogenic centers, and a new double bond were generated in a single chemical operation. Based on this cascade transformation, we achieved a unified strategy toward the stereoselective total syntheses of halimene-type terpenoids and analogues as a proof-of-concept study. This method has been applied to the rapid synthesis of diterpene isotuberculosinol, a virulence factor of Mycobacterium tuberculosis as a representative example.

Characterization of hamster NAD+-dependent 3(17)β-hydroxysteroid dehydrogenase belonging to the aldo-keto reductase 1C subfamily

The cDNAs for morphine 6-dehydrogenase (AKR1C34) and its homologous aldo-keto reductase (AKR1C35) were cloned from golden hamster liver, and their enzymatic properties and tissue distribution were compared. AKR1C34 and AKR1C35 similarly oxidized various xenobiotic alicyclic alcohols using NAD+, but differed in their substrate specificity for hydroxysteroids and inhibitor sensitivity. While AKR1C34 showed 3α/17β/20α-hydroxysteroid dehydrogenase activities, AKR1C35 efficiently oxidized various 3β- and 17β-hydroxysteroids, including biologically active 3β-hydroxy-5α/β-dihydro-C19/C21-steroids, dehydroepiandrosterone and 17β-estradiol. AKR1C35 also differed from AKR1C34 in its high sensitivity to flavonoids, which inhibited competitively with respect to 17β-estradiol (Ki 0.11-0.69 μM). The mRNA for AKR1C35 was expressed liver-specific in male hamsters and ubiquitously in female hamsters, whereas the expression of the mRNA for AKR1C34 displayed opposite sexual dimorphism. Because AKR1C35 is the first 3(17)β-hydroxysteroid dehydrogenase in the AKR superfamily, we also investigated the molecular determinants for the 3β-hydroxysteroid dehydrogenase activity by replacement of Val54 and Cys310 in AKR1C35 with the corresponding residues in AKR1C34, Ala and Phe, respectively. The mutation of Val54Ala, but not Cys310Phe, significantly impaired this activity, suggesting that Val54 plays a critical role in recognition of the steroidal substrate.

GGA AND GGA DERIVATIVES COMPOSITIONS THEREOF AND METHODS FOR TREATING NEURODEGENERATIVE DISEASES INCLUDING PARALYSIS INCLUDING THEM

This invention relates to geranylgeranyl acetone (GGA) derivatives and the use of GGA, its isomers, and GGA derivatives in methods for inhibiting neural death, increasing neural activity, increasing axon growth and cell viability, and increasing the survival rate of subjects administered the GGA or GGA derivatives.

GGA AND GGA DERIVATIVES, COMPOSITIONS THEREOF AND METHODS FOR TREATING NEURODEGENERATIVE DISEASES INCLUDING PARALYSIS INCLUDING THEM

This invention relates to geranylgeranyl acetone (GGA) derivatives and the use of GGA, its isomers, and GGA derivatives in methods for inhibiting neural death, increasing neural activity, increasing axon growth and cell viability, and increasing the survival rate of subjects administered the GGA or GGA derivatives.

Rabbit 3-hydroxyhexobarbital dehydrogenase is a NADPH-preferring reductase with broad substrate specificity for ketosteroids, prostaglandin D2, and other endogenous and xenobiotic carbonyl compounds

3-Hydroxyhexobarbital dehydrogenase (3HBD) catalyzes NAD(P) +-linked oxidation of 3-hydroxyhexobarbital into 3-oxohexobarbital. The enzyme has been thought to act as a dehydrogenase for xenobiotic alcohols and some hydroxysteroids, but its physiological function remains unknown. We have purified rabbit 3HBD, isolated its cDNA, and examined its specificity for coenzymes and substrates, reaction directionality and tissue distribution. 3HBD is a member (AKR1C29) of the aldo-keto reductase (AKR) superfamily, and exhibited high preference for NADP(H) over NAD(H) at a physiological pH of 7.4. In the NADPH-linked reduction, 3HBD showed broad substrate specificity for a variety of quinones, ketones and aldehydes, including 3-, 17- and 20-ketosteroids and prostaglandin D2, which were converted to 3α-, 17β- and 20α-hydroxysteroids and 9α,11β- prostaglandin F2, respectively. Especially, α-diketones (such as isatin and diacetyl) and lipid peroxidation-derived aldehydes (such as 4-oxo- and 4-hydroxy-2-nonenals) were excellent substrates showing low Km values (0.1-5.9 μM). In 3HBD-overexpressed cells, 3-oxohexobarbital and 5β-androstan-3α-ol-17-one were metabolized into 3-hydroxyhexobarbital and 5β-androstane-3α,17β-diol, respectively, but the reverse reactions did not proceed. The overexpression of the enzyme in the cells decreased the cytotoxicity of 4-oxo-2-nonenal. The mRNA for 3HBD was ubiquitously expressed in rabbit tissues. The results suggest that 3HBD is an NADPH-preferring reductase, and plays roles in the metabolisms of steroids, prostaglandin D2, carbohydrates and xenobiotics, as well as a defense system, protecting against reactive carbonyl compounds.

Roles of rat and human aldo-keto reductases in metabolism of farnesol and geranylgeraniol

Farnesol (FOH) and geranylgeraniol (GGOH) with multiple biological actions are produced from the mevalonate pathway, and catabolized into farnesoic acid and geranylgeranoic acid, respectively, via the aldehyde intermediates (farnesal and geranylgeranial). We investigated the intracellular distribution, sequences and properties of the oxidoreductases responsible for the metabolic steps in rat tissues. The oxidation of FOH and GGOH into their aldehyde intermediates were mainly mediated by alcohol dehydrogenases 1 (in the liver and colon) and 7 (in the stomach and lung), and the subsequent step into the carboxylic acids was catalyzed by a microsomal aldehyde dehydrogenase. In addition, high reductase activity catalyzing the aldehyde intermediates into FOH (or GGOH) was detected in the cytosols of the extra-hepatic tissues, where the major reductase was identified as aldo-keto reductase (AKR) 1C15. Human reductases with similar specificity were identified as AKR1B10 and AKR1C3, which most efficiently reduced farnesal and geranylgeranial among seven enzymes in the AKR1A-1C subfamilies. The overall metabolism from FOH to farnesoic acid in cultured cells was significantly decreased by overexpression of AKR1C15, and increased by addition of AKR1C3 inhibitors, tolfenamic acid and R-flurbiprofen. Thus, AKRs (1C15 in rats, and 1B10 and 1C3 in humans) may play an important role in controlling the bioavailability of FOH and GGOH.

Evaluation of morphogenic regulatory activity of farnesoic acid and its derivatives against Candida albicans dimorphism

A series of farnesoic acid derivatives was prepared and their morphogenic regulatory activities were evaluated. Their inhibitory activities against yeast cell growth and yeast-to-hypha transition examined in Candida albicans cells are dependent upon the chain length as well as the substitution patterns on the isoprenoid template. The preliminary structure-activity relationship of these compounds is described to elucidate the essential structural requirements.

Synthesis of allylic isoprenoid diphosphates by S(N)2 displacement of diethyl phosphate

Allylic polyenyl diphosphates such as geranyl and (E,E,E)-geranylgeranyl diphosphates are ubiquitous substrates for monoterpene and diterpene synthases and transferases in isoprenoid biosynthesis. These enzyme substrates were prepared in asymmetrically labeled form by reduction of 1- deuterio aldehyde precursors with (R)- and (S)-Alpine boranes, conversion into diethyl phosphates, and S(N)2 displacements with tris(tetrabutylammonium) pyrophosphate which occurred slowly with essentially complete inversion of configuration over 2-5 days. The 8-α and 8β-hydroxy- 17-nor analogs (13 and 14) of copalyl diphosphate as well as the (15R)- deuterium-labeled form of 13 were similarly prepared from nor-diols 11, (15S)-[15-2H1]-11, and 12 by means of regioselective phosphorylation of the allylic hydroxy groups and displacements with pyrophosphate anion. The configurations and enantiopurities of the deuterium-labeled geraniols, before and after the S(N)2 displacements, and the diastereopurity of the bicyclic keto alcohol intermediate (15S)-[15-2H1]-15 were determined by conversion into (1S)-camphanate esters and 1H-NMR analysis. Amino alcohol 18 was similarly converted into amino diphosphate 19, 15-aza-14,15-dihydro GGPP, a potential aza analog inhibitor for diterpene synthases which generate stereoisomeric forms of copalyl diphosphate.

Concise synthesis of cembrenes based on radical-mediated vinylcyclopropane ring-opening reactions in casbene

Treatment of the bicyclopentadecatriene casbene 1 with ethanethiol radical (EtSH in C6H6, heat) results in regiospecific 1,4-addition to the vinylcyclopropane ring system, producing the cembrene sulfide 10.In similar reactions chrysanthemyl alcohol 11 and carene 13 lead exclusively to the corresponding sulfides 12 and 14, respectively, whereas irradiation of methyl chrysanthemate 15 with ethanethiol produces a 1:1 mixture of the isomeric sulfides 16 and 17.Oxidation of the cembrene sulfide 10, followed by thermolysis of the resulting sulfoxide then produces isocembrene 20, identical with natural material from Pinus sibirica.When a solution of casbene 1 in CCl4 was heated in the presence of NBS and AIBN, it underwent smooth oxidative rearrangement, via 21 and 22, to cembrenene 23, identical with the natural product isolated from the soft coral Sinularia maji.

Biosynthetic precursors for α- and β-cembrenediol formation in tobacco

After survey of the α- and β-cembrenediol (CBD) content of different plant organs of tobacco, calyces were selected for tracer administration. (R/S)-[2-14C]-Mevalonic acid dibenzylethylenediamine salt gave incorporations of 0.10% into α-CBD and 0.03% into gb-CBD. Good incorporations (α-CBD 2.30%, β-CBD 0.93%) of sodium [1-14C] acetate were found. all-(E)-[2-14C]-Geranylgeraniol gave incorporations of 1.49 and 1.53% into the cembrenediols in two experiments, though radiochemical distribution among α- and β- forms was variable. Using the Kato cyclization method, a sample of (R/S)-[3-14C]-cembrene was prepared and was incorporated into the cembrenediols (0.58 and 0.42% overall, with variable distribution among α- and β-isomers). Methods for making (R/S)-[2-2H], [15-2H] and ent- (1R)-[20-3H] cembrene are described. The possible involvement of ent-(1R,3S)-casbene in the formation of (1S)-cembrene is discussed.