Old yellow enzyme-catalysed asymmetric hydrogenation: Linking family roots with improved catalysis

Anika Scholtissek, Dirk Tischler, Adrie H. Westphal, Willem J.H. van Berkel, Caroline E. Paul*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

42 Citations (Scopus)

Abstract

Asymmetric hydrogenation of activated alkenes catalysed by ene-reductases from the old yellow enzyme family (OYEs) leading to chiral products is of potential interest for industrial processes. OYEs’ dependency on the pyridine nucleotide coenzyme can be circumvented through established artificial hydride donors such as nicotinamide coenzyme biomimetics (NCBs). Several OYEs were found to exhibit higher reduction rates with NCBs. In this review, we describe a new classification of OYEs into three main classes by phylogenetic and structural analysis of characterized OYEs. The family roots are linked with their use as chiral catalysts and their mode of action with NCBs. The link between bioinformatics (sequence analysis), biochemistry (structure–function analysis), and biocatalysis (conversion, enantioselectivity and kinetics) can enable an early classification of a putative ene-reductase and therefore the indication of the binding mode of various activated alkenes.
Original languageEnglish
Article number130
JournalCatalysts
Volume7
Issue number5
DOIs
Publication statusPublished - 2017

Keywords

  • Asymmetric hydrogenation
  • Classification of OYE
  • Cofactor analogues
  • Nicotinamide coenzyme biomimetics
  • Old yellow enzymes
  • Oxidoreductases
  • Phylogenetics
  • Selective reduction

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