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Exploring the substrate scope of mutants derived from the robust alcohol dehydrogenase TbSADH

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Sun,  Zhoutong
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Li,  Guangyue
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Ilie,  Adriana
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Citation

Sun, Z., Li, G., Ilie, A., & Reetz, M. T. (2016). Exploring the substrate scope of mutants derived from the robust alcohol dehydrogenase TbSADH. Tetrahedron Letters, 57(32), 3648-3651. doi:10.1016/j.tetlet.2016.06.134.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-2E6F-A
Abstract
Directed evolution of an enzyme as catalyst for a given stereoselective transformation provides a mutant for that particular reaction, but organic chemists need catalysts that are characterized by broad substrate acceptance. In a previous study we succeeded in evolving a set of variants of the thermally robust alcohol dehydrogenase TbSADH from Thermoanaerobacter brockii as a catalysts in the (R)- and (S)-selective reduction of tetrahydrofuran-3-one, this difficult-to-reduce compound being a sterically small substrate. These mutants were now tested in the asymmetric reduction of seven structurally unrelated and sterically more demanding substrates, including acetophenone, benzyl methyl ketone, 4-phenyl-2-butanone, and 2-oxo-4-phenyl-butanoic acid ethyl ester. The variants clearly out-perform WT TbSADH, but overly bulky substituted benzophenone derivatives are not accepted by WT or mutants.