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Enzyme‐Catalyzed Carbonyl Olefination by the <i>E. coli</i> Protein YfeX in the Absence of Phosphines
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Citations
27
References
2016
Year
Carbonyl OlefinationE. ColiEngineeringComplex Molecular ScaffoldsBiochemistryNatural SciencesBiocatalysisEnzyme CatalysisBiotechnologySynthetic BiologyPathway EngineeringStructure-function Enzyme KineticsEnzymatic ModificationChemical BiotechnologyBiomolecular Engineering
Abstract The Wittig‐type carbonyl olefination reaction has no biocatalytic equivalent. To build complex molecular scaffolds, however, C−C bond‐forming reactions are pivotal for biobased economy and synthetic biology. The heme‐containing E. coli protein YfeX was found to catalyze carbonyl olefination by reaction of benzaldehyde with ethyl diazoacetate under aerobic conditions in the absence of a triphenylphosphine oxophile. The reaction was performed in whole cells and showed a product formation of 440 mg L −1 in 1 h. It was, moreover, shown that the reaction could be performed under Wittig‐analogue conditions in the presence of triphenylphosphine or triphenylarsine.
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