62247-44-3

Upstream product

• 108-05-4 vinyl acetate 
• 21378-21-2 3-methylcyclohex-2-en-1-ol 
• 108-22-5 Isopropenyl acetate 
• 75411-49-3 3-methyl-2-cyclohexen-1-yl acetate 
• 108-82-7 2,6-dimethyl-4-heptanol 

Downstream Products

• 914651-24-4 (S)-3-(2-iodoethyl)-3-methylcyclohexene 
• 914651-31-3 (S)-2-{2-[(1R,3R,5R)-3-(tert-butyldimethylsiloxy)-5-isopropyl-1-methyl-2-methylencyclopentyl]ethyl}-2-methylcyclohexanone 
• 914651-29-9 (3R,4R)-4-isopropyl-3-methyl-3-[((S)-1-methylcyclohex-2-en-1-yl)ethyl]-2-methylenecyclopentanone 
• 1026014-56-1 C₂₁HH₃₇OSi 
• 914651-25-5 2-((S)-1-methyl-cyclohex-2-enyl)ethanol 

Relevant academic research and scientific papers

Discovery and Design of Family VIII Carboxylesterases as Highly Efficient Acyltransferases

Promiscuous acyltransferase activity is the ability of certain hydrolases to preferentially catalyze acyl transfer over hydrolysis, even in bulk water. However, poor enantioselectivity, low transfer efficiency, significant product hydrolysis, and limited substrate scope represent considerable drawbacks for their application. By activity-based screening of several hydrolases, we identified the family VIII carboxylesterase, EstCE1, as an unprecedentedly efficient acyltransferase. EstCE1 catalyzes the irreversible amidation and carbamoylation of amines in water, which enabled the synthesis of the drug moclobemide from methyl 4-chlorobenzoate and 4-(2-aminoethyl)morpholine (ca. 20 % conversion). We solved the crystal structure of EstCE1 and detailed structure–function analysis revealed a three-amino acid motif important for promiscuous acyltransferase activity. Introducing this motif into an esterase without acetyltransferase activity transformed a “hydrolase” into an “acyltransferase”.

Enzyme- and ruthenium-catalyzed dynamic kinetic resolution of functionalized cyclic allylic alcohols

Enantioselective synthesis of functionalized cyclic allylic alcohols via dynamic kinetic resolution has been developed. Cyclopentadienylruthenium catalysts were used for the racemization, and lipase PS-IM or CALB was employed for the resolution. By optimization of the reaction conditions the formation of the enone byproduct was minimized, making it possible to prepare a range of optically active functionalized allylic alcohols in good yields and high ee's.

The Candida antarctica lipase B catalysed kinetic resolution of seudenol in non-aqueous media of controlled water activity

For further ivestigation of the kinetic resolutions in transesterification reactions with the highly enantioselective Candida antarctica lipase B, an easy to study model reaction with one typical substrate, the Douglas Fir Beetle pheromone 3-methyl-2-cycl

Enzymatic Kinetic Resolution of 2-Cyclohexen-1-ol Derivatives

Optically active (S)-2-cyclohexen-1-ol derivatives and their enantiomeric (R)-acetates have been obtained in high enantiomeric excesses by enzymatic kinetic acetylation catalyzed by lipase AK.

Pheromone Synthesis, CXI. - An Enzyme-Mediated Synthesis of Both Enantiomers of Seudenol and 1-Methyl-2-cyclohexen-1-ol, the Aggregation Pheromones of Dendroctonus pseudotsugae

Enzymatic resolution of seudenol acetate by pig liver esterase has led to an efficient preparation of both the enantiomers of seudenol and 1-methyl-2-cyclohexen-1-ol, the aggregation pheromones of the Douglas-fir beetle Dendroctonus pseudotsugae Hopkins.