Lipase-catalyzed kinetic resolution of racemic 1-heteroarylethanols—experimental and QM/MM study
| Autor: | Florin Dan Irimie, György Szakács, Paula Moldovan, Lajos Novák, Csaba Paizs, Monica Ioana Toşa, Gábor Szatzker, László Poppe, Sarolta Pilbák |
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| Rok vydání: | 2008 |
| Předmět: |
biology
Chemistry Stereochemistry Organic Chemistry Acetaldehyde biology.organism_classification Catalysis Kinetic resolution Inorganic Chemistry Acylation QM/MM chemistry.chemical_compound Tetrahedral carbonyl addition compound biology.protein Candida antarctica Physical and Theoretical Chemistry Enantiomer Lipase |
| Zdroj: | Tetrahedron: Asymmetry. 19:1844-1852 |
| ISSN: | 0957-4166 |
| DOI: | 10.1016/j.tetasy.2008.07.004 |
| Popis: | The kinetic resolution of racemic 1-(benzothiazol-2-yl)ethanol rac-2a, 1-(benzo[b]thiophen-2-yl)ethanol rac-2b, 1-(benzo[b]furan-3-yl)ethanol rac-2c and 1-(benzo[b]thiophen-3-yl)ethanol rac-2d was studied by enantiomer selective acylation catalyzed by a selection of commercially available and in house produced lipases. Alcoholysis of the corresponding racemic acetates rac-3a–d catalyzed by Candida antarctica lipase B (CaLB) was also investigated. Two racemic 1-heteroarylethanols rac-2a,b were prepared by addition of the corresponding lithiated heteroarylic compounds 1a,b to acetaldehyde, whereas two others, rac-2c,d were synthesized by the addition of MeMgI onto the corresponding heteroaryl-carbaldehydes 1c,d. The high enantiomer selectivities of CaLB in the acylation of racemic 1-heteroarylethanols rac-2a–d allowed the determination of the enantiomeric preference of these enzymatic acetylation reactions by QM/MM [pm3/uff or hf(3-21+g∗∗)/uff] calculations. For acetylation of each of the racemic alcohols rac-2a–d, four possible tetrahedral intermediate states were compared and analyzed. |
| Databáze: | OpenAIRE |
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