Biocatalytic Michael-Type Additions of Acetaldehyde to Nitroolefins with the Proline-Based Enzyme 4-Oxalocrotonate Tautomerase Yielding Enantioenriched γ-Nitroaldehydes

Edzard M. Geertsema, Yufeng Miao, Pieter G. Tepper, Pim de Haan, Ellen Zandvoort, Gerrit J. Poelarends*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

44 Citations (Scopus)

Abstract

Call me Michaelase: The enzyme 4-oxalocrotonate tautomerase (4-OT) promiscuously catalyzes the Michael-type addition of acetaldehyde to a collection of aromatic and aliphatic nitro-olefins with high stereoselectivity producing precursors of g-aminobutyric acid (GABA) analogues (see scheme).

Original languageEnglish
Pages (from-to)14407-14410
Number of pages4
JournalChemistry
Volume19
Issue number43
DOIs
Publication statusPublished - 18-Oct-2013

Keywords

  • aminobutyric acid
  • biocatalysis
  • C-C bond formation
  • enzymes
  • Michael-type addition
  • DIPHENYLPROLINOL SILYL ETHER
  • PLACEBO-CONTROLLED TRIAL
  • CARBON BOND FORMATIONS
  • ALPHA,BETA-UNSATURATED ALDEHYDES
  • 1,4-ADDITION REACTIONS
  • BACLOFEN
  • SUPERFAMILY
  • PREGABALIN
  • CATALYSTS
  • ROLIPRAM

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