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• 141946-97-6 (R,S)-1,1,1-trifluoro-2-phenylbut-3-yn-2-yl acetate 

Relevant academic research and scientific papers

Cross-linked crystals of Candida rugosa lipase: Highly efficient catalysts for the resolution of chiral esters

To date, most enzyme-based organic syntheses have employed enzymes in the form of a crude protein extract. The instability and expense of highly purified proteins has all but obviated their use as catalysts for enantioselective hydrolyses. Herein, we describe the use of the major hydrolase from commercial Candida rugosa lipase (CRL) in the form of a cross-linked enzyme crystal (CLEC) for the enantioselective hydrolysis of chiral racemic esters. The enantioselectivity of CRL-CLECs in the hydrolysis of many important chiral esters is vastly superior to that of the crude CRL extract. Since the CRL-CLEC is insoluble, recoverable, and 2-3 orders of magnitude more stable than the soluble protein, the CRL-CLEC is an attractive replacement for the crude enzyme preparation. The use of this catalyst in the resolution of chiral esters 1-11 and in the preparative scale (1a) and multicycle resolution (2a) of important anti-inflammatory drugs is described.

Characterization of a novel esterase isolated from intertidal flat metagenome and its tertiary alcohols synthesis

A gene coding for an esterase (EstEH112) was isolated from metagenome originated from Korean intertidal flat sediment. The putative esterase gene encoded a 340 amino acids protein with characteristic residues of lipolytic enzymes such as a conserved pentapeptide (GXSXG), the typical catalytic S-D-H triad, and a GGG(A)X-motif in the oxyanion hole near the active site similar to the hormone sensitive lipase (HSL) family. p-Nitrophenyl butyrate was the best substrate for the enzyme among the other p-nitrophenyl esters investigated. The apparent optimal temperature and pH for EstEH112 was 35°C and at pH 8.0, respectively. EstEH112 efficiently catalyzed the hydrolysis of various large tertiary alcohol esters. These characteristics of EstEH112 make it a potential candidate for application in biocatalysis.

Hydrolase-catalyzed stereoselective preparation of protected α,α-dialkyl-α-hydroxycarboxylic acids

The title compounds were prepared by a Passerini multi-component reaction and subjected to enzymatic kinetic resolution using 40 enzymes known to be active towards esters of tertiary alcohols. This identified a protease (P1), a thermophilic esterase (PestE) and an esterase of metagenome origin (esterase 8) as the most active and enantioselective biocatalysts. After further optimization of reaction conditions, two compounds were prepared in preparative scale using esterase 8 yielding (+)-1-(tert-butylamino)-2-methyl-1-oxobutyl-2-yl acetate with 93%ee and (-)-1-(tert-butylamino)-2-trifluoro-methyl-1-oxobutyl-2-yl acetate with 47%ee.

Complete inversion of enantioselectivity towards acetylated tertiary alcohols by a double mutant of a Bacillus subtilis esterase

(Chemical Equation Presented) Simultaneous saturation mutagenesis at three amino acid residues of esterase BS2 followed by high-throughput screening identified a double mutant (E188W/M193C) with inverted enantiopreference, high E values, and broadened sub

Highly enantioselective synthesis of arylaliphatic tertiary alcohols using mutants of an esterase from Bacillus subtilis

The kinetic resolution of a series of acetates of arylaliphatic tertiary alcohols was studied using recombinant esterase variants from Bacillus subtilis (BS2) expressed in E. coli. Highest enantioselectivities (E > 100) were achieved in the synthesis of 1

Hydrolytic Resolution of Tertiary Acetylenic Acetate Esters With the Lipase from Candida Cylindracea

The kinetic resolution of a series of tertiary acetylenic acetate esters using the lipase from Candida cylindracea has been explored.Compounds 6c and the trifluoromethyl acetate 6e have been resolved with high enantiomeric enrichment.Several other tertiary acetate esters carrying a CF3 group have been investigated which proved inert to enzymatic hydrolysis.From these results and published data, we are able to propose a predictive model for identifying the preferred enantiomer of secondary and tertiary trifluoromethyl acetate esters for this lipase.