Bridging between Organocatalysis and Biocatalysis: Asymmetric Addition of Acetaldehyde to β-Nitrostyrenes Catalyzed by a Promiscuous Proline-Based Tautomerase

Non‐natural beauty: The enzyme 4‐oxalocrotonate tautomerase (4‐OT) promiscuously (i.e., with non‐natural activity) catalyzes the Michael‐type addition of acetaldehyde to nitrostyrene. Catalysis likely proceeds via enamine formation of the amino‐terminal proline residue of 4‐OT with acetaldehyde (see...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2012-01, Vol.51 (5), p.1240-1243
Main Authors: Zandvoort, Ellen, Geertsema, Edzard M., Baas, Bert-Jan, Quax, Wim J., Poelarends, Gerrit J.
Format: Article
Language:English
Subjects:
Acetaldehyde - chemistry
Biocatalysis
Catalysis
catalytic promiscuity
enzyme catalysis
Isomerases - chemistry
Isomerases - metabolism
Michael addition
organocatalysis
Proline - chemistry
Styrenes - chemistry
tautomerases
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Summary:Non‐natural beauty: The enzyme 4‐oxalocrotonate tautomerase (4‐OT) promiscuously (i.e., with non‐natural activity) catalyzes the Michael‐type addition of acetaldehyde to nitrostyrene. Catalysis likely proceeds via enamine formation of the amino‐terminal proline residue of 4‐OT with acetaldehyde (see picture), reminiscent of organocatalysis. High stereoselectivity, low catalyst loading, and water as reaction medium characterize this methodology.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201107404