Overcoming co-product inhibition in the nicotinamide independent asymmetric bioreduction of activated C=C-bonds using flavin-dependent ene-reductases

Biotechnol Bioeng. 2013 Dec;110(12):3085-92. doi: 10.1002/bit.24981. Epub 2013 Jul 10.

Abstract

Eleven flavoproteins from the old yellow enzyme family were found to catalyze the disproportionation ("dismutation") of conjugated enones. Incomplete conversions, which were attributed to enzyme inhibition by the co-product phenol could be circumvented via in situ co-product removal by scavenging the phenol using the polymeric adsorbent MP-carbonate. The optimized system allowed to reduce an alkene activated by ester groups in a "coupled-substrate" approach via nicotinamide-free hydrogen transfer with >90% conversion and complete stereoselectivity.

Keywords: disproportionation; ene-reductase; in situ co-product removal; old yellow enzyme.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkanes / metabolism*
  • Coenzymes / metabolism*
  • Dinitrocresols / metabolism*
  • Enzyme Inhibitors / metabolism
  • Flavoproteins / metabolism*
  • Niacinamide / metabolism
  • Oxidation-Reduction
  • Oxidoreductases / metabolism*
  • Phenol / metabolism

Substances

  • Alkanes
  • Coenzymes
  • Dinitrocresols
  • Enzyme Inhibitors
  • Flavoproteins
  • 4,6-dinitro-o-cresol
  • Niacinamide
  • Phenol
  • Oxidoreductases