Back Cover: Enzyme-Catalyzed Carbonyl Olefination by the E. coli Protein YfeX in the Absence of Phosphines (ChemCatChem 9/2016)

The Cover shows an enzymatic carbonyl olefination reaction in E.coli where the corresponding enzyme—depicted as the clownfish nemo—has to be found in the organism which is represented by the ocean. In their paper, Weissenborn, Löw et al. present a method to find new enzyme activities by utilizing an...

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Veröffentlicht in:	ChemCatChem 2016-05, Vol.8 (9), p.1747-1747
Hauptverfasser:	Weissenborn, Martin J., Löw, Sebastian A., Borlinghaus, Niels, Kuhn, Miriam, Kummer, Stefanie, Rami, Fabian, Plietker, Bernd, Hauer, Bernhard
Format:	Artikel
Sprache:	eng
Schlagworte:	biocatalysis C−C bond formation enzyme catalysis olefination Wittig reactions
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creator	Weissenborn, Martin J. Löw, Sebastian A. Borlinghaus, Niels Kuhn, Miriam Kummer, Stefanie Rami, Fabian Plietker, Bernd Hauer, Bernhard
description	The Cover shows an enzymatic carbonyl olefination reaction in E.coli where the corresponding enzyme—depicted as the clownfish nemo—has to be found in the organism which is represented by the ocean. In their paper, Weissenborn, Löw et al. present a method to find new enzyme activities by utilizing an entire cell lysate with its thousands of proteins as catalyst. Once they found that the cell lysate catalyzes a carbonyl olefination reaction they determined, isolated, and studied the corresponding protein. The results show the first enzymatic carbonyl olefination in absence of phosphines, as well as the feasibility of the performed general approach in cell lysates. More information can be found in the Communication by Weissenborn, Löw et al. on page 1636 in Issue 9, 2016 (DOI: 10.1002/cctc.201600227).
doi_str_mv	10.1002/cctc.201600483
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subjects	biocatalysis C−C bond formation enzyme catalysis olefination Wittig reactions
title	Back Cover: Enzyme-Catalyzed Carbonyl Olefination by the E. coli Protein YfeX in the Absence of Phosphines (ChemCatChem 9/2016)
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