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

doi:10.1002/chem.201302351

Biocatalytic Michael-type additions of acetaldehyde to nitroolefins with the proline-based enzyme 4-oxalocrotonate tautomerase yielding enantioenriched γ-nitroaldehydes

Chemistry. 2013 Oct 18;19(43):14407-10. doi: 10.1002/chem.201302351. Epub 2013 Sep 24.

Authors

Edzard M Geertsema¹, Yufeng Miao, Pieter G Tepper, Pim de Haan, Ellen Zandvoort, Gerrit J Poelarends

Affiliation

¹ Department of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen (The Netherlands).

PMID: 24115023
DOI: 10.1002/chem.201302351

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 nitroolefins with high stereoselectivity producing precursors of γ-aminobutyric acid (GABA) analogues.

Keywords: C-C bond formation; Michael-type addition; aminobutyric acid; biocatalysis; enzymes.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acetaldehyde / chemistry
Acetaldehyde / metabolism*
Alkenes / chemistry
Alkenes / metabolism*
Biocatalysis
Carbon / chemistry
Isomerases / metabolism*
Nitro Compounds / chemistry*
Proline / chemistry*
Stereoisomerism
gamma-Aminobutyric Acid / metabolism

Substances

Alkenes
Nitro Compounds
gamma-Aminobutyric Acid
Carbon
Proline
4-oxalocrotonate tautomerase
Isomerases
Acetaldehyde