NAD(P)H-independent asymmetric C=C bond reduction catalyzed by ene reductases by using artificial co-substrates as the hydrogen donor

Chemistry. 2014 Jan 27;20(5):1403-9. doi: 10.1002/chem.201303897. Epub 2013 Dec 30.

Abstract

To develop a nicotinamide-independent single flavoenzyme system for the asymmetric bioreduction of C=C bonds, four types of hydrogen donor, encompassing more than 50 candidates, were investigated. Six highly potent, cheap, and commercially available co-substrates were identified that (under the optimized conditions) resulted in conversions and enantioselectivities comparable with, or even superior to, those obtained with traditional two-enzyme nicotinamide adenine dinucleotide phosphate (NAD(P)H)-recycling systems.

Keywords: alkene reduction; artificial biocatalysis; ene reductases; enzyme catalysis; hydrogen donors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biocatalysis
  • Biocompatible Materials / chemistry
  • Biocompatible Materials / metabolism
  • Carbon / chemistry
  • Hydrogen / chemistry*
  • NAD / chemistry*
  • Oxidation-Reduction
  • Oxidoreductases / chemistry
  • Oxidoreductases / metabolism*
  • Stereoisomerism
  • Substrate Specificity

Substances

  • Biocompatible Materials
  • NAD
  • Carbon
  • Hydrogen
  • Oxidoreductases