Bioorthogonal Enzymatic Activation of Caged Compounds
| Autor: | Peter L. Graumann, Eric Meggers, Katja Kräling, Nathalie Nett, Manfred T. Reetz, Felix Dempwolff, Cornelia Ritter, Carlos G. Acevedo-Rocha, Richard Lonsdale, Sabrina Hoebenreich |
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| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular Molecular Structure Ether General Chemistry Protein engineering Monooxygenase Directed evolution Protein Engineering Combinatorial chemistry Catalysis Enzyme Activation chemistry.chemical_compound chemistry Cytochrome P-450 Enzyme System Docking (molecular) Alcohols Escherichia coli Bioorthogonal chemistry Selectivity Protecting group Ethers |
| Zdroj: | Angewandte Chemie (International ed. in English). 54(45) |
| ISSN: | 1521-3773 |
| Popis: | Engineered cytochrome P450 monooxygenase variants are reported as highly active and selective catalysts for the bioorthogonal uncaging of propargylic and benzylic ether protected substrates, including uncaging in living E. coli. observed selectivity is supported by induced-fit docking and molecular dynamics simulations. This proof-of-principle study points towards the utility of bioorthogonal enzyme/protecting group pairs for applications in the life sciences. |
| Databáze: | OpenAIRE |
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