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Biocatalysts for the pharmaceutical industry created by structure-guided directed evolution of stereoselective enzymes

MPG-Autoren

Li,  Guangyue
Fachbereich Chemie, Philipps-Universität;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Wang,  Jianbo
Fachbereich Chemie, Philipps-Universität;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Reetz,  Manfred T.
Fachbereich Chemie, Philipps-Universität;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Zitation

Li, G., Wang, J., & Reetz, M. T. (2018). Biocatalysts for the pharmaceutical industry created by structure-guided directed evolution of stereoselective enzymes. Bioorganic & Medicinal Chemistry, 26(7), 1241-1251. doi:10.1016/j.bmc.2017.05.021.


Zitierlink: http://hdl.handle.net/21.11116/0000-0001-49CE-6
Zusammenfassung
Enzymes have been used for a long time as catalysts in the asymmetric synthesis of chiral intermediates needed in the production of therapeutic drugs. However, this alternative to man-made catalysts has suffered traditionally from distinct limitations, namely the often observed wrong or insufficient enantio- and/or regioselectivity, low activity, narrow substrate range, and insufficient thermostability. With the advent of directed evolution, these problems can be generally solved. The challenge is to develop and apply the most efficient mutagenesis methods which lead to highest-quality mutant libraries requiring minimal screening. Structure-guided saturation mutagenesis and its iterative form have emerged as the method of choice for evolving stereo- and regioselective mutant enzymes needed in the asymmetric synthesis of chiral intermediates. The number of (industrial) applications in the preparation of chiral pharmaceuticals is rapidly increasing. This review features and analyzes typical case studies.