A conserved threonine prevents self-intoxication of enoyl-thioester reductases

May 15th, 2017 by Raoul G Rosenthal

Nature Chemical Biology 13, 745 (2017). doi:10.1038/nchembio.2375

Authors: Raoul G Rosenthal, Bastian Vögeli, Tristan Wagner, Seigo Shima & Tobias J Erb

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

April 13th, 2015 by Raoul G Rosenthal

Nature Chemical Biology 11, 398 (2015). doi:10.1038/nchembio.1794

Authors: Raoul G Rosenthal, Bastian Vögeli, Nick Quade, Guido Capitani, Patrick Kiefer, Julia A Vorholt, Marc-Olivier Ebert & Tobias J Erb

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.

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