2002年6月
Mechanism-based enzymatic method for reliable determination of absolute configuration of chiral 1-substituted ethanols: combination with NMR method
TETRAHEDRON-ASYMMETRY
- ,
- ,
- ,
- 巻
- 13
- 号
- 11
- 開始ページ
- 1223
- 終了ページ
- 1229
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1016/S0957-4166(02)00318-X
- 出版者・発行元
- PERGAMON-ELSEVIER SCIENCE LTD
It has been demonstrated that lipase is useful not only for kinetic resolution but also for the rapid determination of absolute configurations. We have previously proposed a mechanism represented by transition-state models to rationalize the enantioselectivity in the lipase- and subtilisin-catalyzed kinetic resolutions of secondary alcohols. The mechanism indicates that the enzyme-catalyzed reactions can be used as a tool for determining the absolute stereochemistry of secondary alcohols. In order to increase reliability, the enzymatic method was combined with Mosher's method using MTPA, to give a protocol which is named the double-confirmation method. The absolute configurations of six 1-substituted ethanols were determined consistently by this new procedure. The enzymatic method is quick, easy, economical, and reliable. An interesting similarity in conformation between the transition-state models and MTPA esters is also described. (C) 2002 Elsevier Science Ltd. All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/S0957-4166(02)00318-X
- ISSN : 0957-4166
- CiNii Articles ID : 80015449126
- Web of Science ID : WOS:000177072100018