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The use of ene adducts to study and engineer enoyl-thioester reductases

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Rosenthal,  R.
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zurich, Zurich, Switzerland;

/persons/resource/persons254801

Vögeli,  B.
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zurich, Zurich, Switzerland;

/persons/resource/persons254247

Erb,  T. J.
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zurich, Zurich, Switzerland;

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https://www.ncbi.nlm.nih.gov/pubmed/25867044
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Citation

Rosenthal, R., Vögeli, B., Quade, N., Capitani, G., Kiefer, P., Vorholt, J. A., et al. (2015). The use of ene adducts to study and engineer enoyl-thioester reductases. Nat Chem Biol, 11(6), 398-400. doi:10.1038/nchembio.1794.


Cite as: https://hdl.handle.net/21.11116/0000-000A-CB01-0
Abstract
An improved understanding of enzymes' catalytic proficiency and stereoselectivity would further enable applications in chemistry, biocatalysis and industrial biotechnology. We use a chemical probe to dissect individual catalytic steps of enoyl-thioester reductases (Etrs), validating an active site tyrosine as the cryptic proton donor and explaining how it had eluded definitive identification. This information enabled the rational redesign of Etr, yielding mutants that create products with inverted stereochemistry at wild type-like turnover frequency.