Lipase-mediated kinetic resolution of allylic(hydroxymethyl)methylenecyclopentane building blocks |
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| Institution: | 1. Department of Medical Biology, Kocaeli University School of Medicine, 41380 Kocaeli, Turkey;2. DEKART Proteomics Laboratory, Kocaeli University School of Medicine, 41380 Kocaeli, Turkey;3. Department of Biomedical Engineering, Kocaeli University School of Technology, 41380 Kocaeli, Turkey;4. TUBITAK Marmara Research Center, Genetic Engineering and Biotechnology Institute (GEBI), Gebze, 41470 Kocaeli, Turkey;5. Department of Neurology, Kocaeli University School of Medicine, 41380 Kocaeli, Turkey;1. Department of Economics, Business and Statistics, University of Palermo, Viale delle Scienze Ed. 13, Palermo, Italy;2. Department of Political Science, University of Roma Tre, Via G. Chiabrera, 199, Rome, Italy |
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| Abstract: | Enzymatic-mediated kinetic acylation of allylic(hydroxymethyl)methylenecyclopentane building blocks (±)-1a,b is reported using various commercially available lipases. Lipase Amano AK (Pseudomonas sp.) proved to be the best lipase in the case of (?)-1b which was obtained with a 96% enantiomeric excess. Single crystal X-ray diffraction analysis, using the (1S,4R)-camphanate derivative of (?)-1b, helped us to assign the S absolute configuration of (?)-1b and the enantiomeric specificity of the tested lipases. |
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