Mechanism-based enzymatic method for reliable determination of absolute configuration of chiral 1-substituted ethanols: Combination with NMR method

Tadashi Ema, Masataka Yoshii, Toshinobu Korenaga, Takashi Sakai

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17 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1223-1229
Number of pages7
JournalTetrahedron Asymmetry
Volume13
Issue number11
DOIs
Publication statusPublished - Jun 21 2002

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ASJC Scopus subject areas

  • Inorganic Chemistry
  • Organic Chemistry
  • Materials Chemistry
  • Drug Discovery

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