Chemoenzymatic Dynamic Kinetic Asymmetric Transformations of β-Hydroxyketones

Chemistry. 2021 Nov 11;27(63):15623-15627. doi: 10.1002/chem.202102683. Epub 2021 Oct 5.

Abstract

Herein we report on the development and application of chemoenzymatic Dynamic Kinetic Asymmetric Transformation (DYKAT) of α-substituted β-hydroxyketones (β-HKs), using Candida antartica lipase B (CALB) as transesterification catalyst and a ruthenium complex as epimerization catalyst. An operationally simple protocol allows for an efficient preparation of highly enantiomerically enriched α-substituted β-oxoacetates. The products were obtained in yields up to 95 % with good diastereomeric ratios.

Keywords: DYKAT; lipase; racemization; ruthenium; β-hydroxyketones.

MeSH terms

  • Catalysis
  • Fungal Proteins
  • Kinetics
  • Lipase / metabolism
  • Ruthenium*
  • Stereoisomerism

Substances

  • Fungal Proteins
  • Ruthenium
  • Lipase
  • lipase B, Candida antarctica