74742-10-2

Upstream product

• 124-19-6 nonan-1-al 
• 544-97-8 dimethyl zinc(II) 
• 1120-06-5 decan-2-ol 
• 693-54-9 Decan-2-one 
• 94340-16-6 (2R,4R)-4-(1-Methyl-nonyloxy)-pentan-2-ol 
• 94340-16-6 (2S,4S)-4-(1-Methyl-nonyloxy)-pentan-2-ol 
• 865711-50-8 decan-2-yl acetate 
• 1000995-40-3 1-methyl-3-(11-ethoxycarbonyl-undecyl)imidazolium hexafluorophosphate 
• 75-16-1 methylmagnesium bromide 
• 124-18-5 decane 
• 629-04-9 1-Bromoheptane 
• 15448-47-2 (R)-propylene oxide 
• 94340-13-3 (4S,6S)-4,6-Dimethyl-2-octyl-[1,3]dioxane 
• 85028-98-4 (4R,6R)-4,6-dimethyl-2-octyl-1,3-dioxane 

Downstream Products

• 1120-06-5 decan-2-ol 
• 1333311-39-9 1-((S)-decan-2-yloxy)-4-iodobenzene 
• 1284282-05-8 1,3,5-tris(2-(4-((S)-decan-2-yloxy)phenyl)ethynyl)benzene 
• 1393538-47-0 (S)-2-methyl-1-(4-methylphenylsulfonyl)decane 
• 1393538-58-3 (5S,9S)-5,9-dimethyl-8-(4-methylphenylsulfonyl)heptadecane 
• 1393538-59-4 (5R,9S)-5,9-dimethyl-8-(4-methylphenylsulfonyl)heptadecane 
• 108195-53-5 (5S,9S)-5,9-Dimethylheptadecane 
• 130566-82-4 (R)-2-decanyl tosylate 
• 1175669-90-5 C₂₂H₃₆O₇S 

Relevant academic research and scientific papers

Highly enantioselective synthesis of long chain alkyl trifluoromethyl carbinols and β-thiotrifluoromethyl carbinols through lipases

Among a variety of lipases tested, Candida antarctica lipase has been found to promote the enantioselective acylation of long chain alkyl trifluoromethyl carbinols 1a-4a and β-thiotrifluoromethyl carbinols 5a-7a, producing both R and S enantiomeric alcohols in good to excellent chemical yield and enantioselectivity. In all cases the lipase preferentially acylates the S enantiomer, irrespective the presence or not of a sulfur atom in β position to the hydroxyl group. When the reaction was carried out on the non-fluorinated substrates 1c-2c, the process occurred much faster and with higher e.e. of the less reacting enantiomer than when conducted on the fluorinated substrates.

Identification of a Robust Carbonyl Reductase for Diastereoselectively Building syn-3,5-Dihydroxy Hexanoate: A Bulky Side Chain of Atorvastatin

t-Butyl-6-cyano-(3R,5R)-dihydroxyhexanoate is an advanced chiral precursor for the synthesis of the side chain pharmacophore of cholesterol-lowering drug atorvastatin. Herein, a robust carbonyl reductase (LbCR) was newly identified from Lactobacillus brevis, which displays high activity and excellent diastereoselectivity toward bulky t-butyl 6-cyano-(5R)-hydroxy-3-oxo-hexanoate (7). The engineered Escherichia coli cells harboring LbCR and glucose dehydrogenase (for cofactor regeneration) were employed as biocatalysts for the asymmetric reduction of substrate 7. As a result, as much as 300 g L-1 of water-insoluble substrate was completely converted to the corresponding chiral diol with >99.5% de in a space-time yield of 351 g L-1 d-1, indicating a great potential of LbCR for practical synthesis of the very bulky and bi-chiral 3,5-dihydroxy carboxylate side chain of best-selling statin drugs.

A novel P450-based biocatalyst for the selective production of chiral 2-alkanols

A P450 monooxygenase from Nocardia farcinica (CYP154A8) catalyses the stereo- and regioselective hydroxylation of n-alkanes, still a challenging task in chemical catalysis. In a biphasic reaction system, the regioselectivity for the C2-position of C7-C9 alkanes was over 90%. The enzyme showed strict S-selectivity for all tested substrates, with enantiomeric excess (ee) of up to 91%. This journal is the Partner Organisations 2014.

Continuous biphasic enzymatic reduction of aliphatic ketones

Biphasic reactions offer an attractive alternative for the utilisation of enzymes for conversion of hardly water soluble substrates. Especially, the alcohol dehydrogenase from Lactobacillus brevis was successfully used for the reductive synthesis of enantiopure secondary aliphatic alcohols. With the enzymatic catalyst and the cofactor effectively retained in the reactive aqueous phase, the continuous operation was demonstrated by continuous addition and withdrawal of the non-reactive phase. The four tested substrates 2-heptanone, 2-octanone, 2-nonanone, and 2-decanone showed that the space time yield and turnover numbers (TON) of the enzyme decrease as the availability of the substrate decreases with increasing partition coefficients. Nevertheless, a TONLbADH of up to 478 × 103 could be achieved. Remarkably, the cofactor utilisation turned out to be very high and a TON NADP+ of more than 20 × 103 was easily achievable for both 2-heptanone and 2-octanone by substrate coupled cofactor regeneration with excess of 2-propanol.

Catalytic enantioselective addition of alkyl grignard reagents to aliphatic aldehydes

Herein, we report an efficient catalytic system for the enantioselective addition of alkyl Grignard reagents to a broad range of aliphatic aldehydes with good yields and enantioselectivities. Remarkably, the challenging methylmagnesium bromide (MeMgBr) can also be added to a variety of aliphatic aldehydes, providing versatile chiral methyl carbinol units with unprecedented yields and enantioselectivities in a simple one-pot procedure under mild conditions. Copyright

Stereospecific inversion of secondary tosylates to yield chiral methyl-branched building blocks, applied to the asymmetric synthesis of leafminer sex pheromones

All four of the possible stereoisomers of 5,9-dimethylheptadecane, the major sex pheromone component secreted by female moths of the mountain-ash bentwing (Leucoptera scitella), were synthesized by the coupling of two chiral blocks with a methyl branch at the 2- or 3-position. The blocks were prepared by applying the stereospecific inversion of secondary tosylates, which were derived from (R)- and (S)-propylene oxide, and their enantiopurities were confirmed by chiral HPLC analysis.

Ionic liquid facilitates biocatalytic conversion of hardly water soluble ketones

Ionic liquids represent a promising alternative to conventional cosolvents as biocompatible solubilisers for biocatalysis. This was shown using water miscible ionic liquids to facilitate the stereoselective reduction of hardly water soluble, aliphatic ketones catalysed by the alcohol dehydrogenase from Lactobacillus brevis. Ten ionic liquids were screened for activity and solubility. Improved storage stabilities besides improved enzyme activities, as well as reduced substrate surplus and product inhibitions were found, while applying the most promising AMMOENG 101 in more detailed investigations. Batch reactions with cofactor regeneration via a glucose dehydrogenase showed increased reaction rates; thus underlining the positive influence of AMMOENG 101. For (R)-3-octanol, (R)-2-nonanol, (R)-2-decanol, and (R)-2-octanol space time yields between 250 and 350 mmol L-1 d -1 were achieved.

Utilising hardly-water soluble substrates as a second phase enables the straightforward synthesis of chiral alcohols

So far, the alcohol dehydrogenase-catalysed conversion of longer chain aliphatic substrates has been challenging due to their low solubility in aqueous solution. However, by utilising the ketone directly as a second organic phase, the straightforward synthesis of long chain aliphatic chiral alcohols is enabled. The Royal Society of Chemistry.

Orchestration of concurrent oxidation and reduction cycles for stereoinversion and deracemisation of sec-alcohols

Black and white are opposites as are oxidation and reduction. Performing an oxidation, for example, of a sec-alcohol and a reduction of the corresponding ketone in the same vessel without separation of the reagents seems to be an impossible task. Here we show that oxidative cofactor recycling of NADP + and reductive regeneration of NADH can be performed simultaneously in the same compartment without significant interference. Regeneration cycles can be run in opposing directions beside each other enabling one-pot transformation of racemic alcohols to one enantiomer via concurrent enantioselective oxidation and asymmetric reduction employing defined alcohol dehydrogenases with opposite stereo- and cofactor-preference. Thus, by careful selection of appropriate enzymes, NADH recycling can be performed in the presence of NADP+ recycling to achieve overall, for example, deracemisation of sec-alcohols or stereoinversion representing a possible concept for a "green" equivalent to the chemical-intensive Mitsunobu inversion.

Deracemization of secondary alcohols through a concurrent tandem biocatalytic oxidation and reduction

(Chemical Equation Presented) Breaking the mirror: A purified alcohol dehydrogenase (ADH) for stereoselective reduction and whole cells of a microorganism for enantioselective oxidation operated concurrently to effect the stereoinversion of one enantiomer of a racemic secondary alcohol and provide the optically pure alcohol in >99% yield (see scheme). R,R′ = alkyl.