Lipase-promoted kinetic resolution of racemic,P-chiral hydroxymethylphosphonates and phosphinates |
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| Institution: | 1. Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan;2. JST, ERATO, Lipid Active Structure Project, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan;3. Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan;1. School of Physics, Shandong University, Jinan 250100, PR China;2. Key Laboratory of Materials for High Power Laser, Shanghai Institute of Optics and Fine Mechanics, Chinese Academy of Sciences, Shanghai 201800, China;1. Department of Basic Science, Graduate School of Arts and Sciences, The University of Tokyo, Komaba, Meguro, Tokyo, 153-8902, Japan;2. Determent of Creative Research, Exploratory Research Center on Life and Living Systems (ExCELLS), Myodaiji, Okazaki, Aichi, 444-8585, Japan;3. Department of Chemistry, Faculty of Science, Kanagawa University, Tsuchiya, Hiratsuka, Kanagawa, 259-1293, Japan;4. Research Center for Complex Systems Biology, The University of Tokyo, Komaba, Meguro, Tokyo, 153-8902, Japan |
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| Abstract: | Lipase-mediated acetylation of racemic P-chiral hydroxymethylphosphonates and phosphinates, and hydrolysis of their O-acetyl derivatives have been conducted under kinetic resolution conditions to give the enantiomerically enriched title products with up to 92% ee. Their absolute configuration has been determined by means of chemical correlation and CD measurements. |
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