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β-Lactones as Privileged Structures for the Active-Site Labeling of Versatile Bacterial Enzyme Classes

Authors

  • Thomas Böttcher,

    1. Center for integrated Protein Science Munich, CiPSM, Department of Chemistry and Biochemistry, Ludwig-Maximilians-Universität München, Butenandtstrasse 5–13, 81377 Munich, Germany, Fax: (+49) 89-2180-77756
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  • Stephan A. Sieber Dr.

    1. Center for integrated Protein Science Munich, CiPSM, Department of Chemistry and Biochemistry, Ludwig-Maximilians-Universität München, Butenandtstrasse 5–13, 81377 Munich, Germany, Fax: (+49) 89-2180-77756
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  • We thank Prof. Thomas Carell and his group for their generous support and fruitful scientific discussions. We gratefully acknowledge funding by the Emmy Noether Program of the DFG), the SFB 749 (DFG grant), a stipend from the Römer Stiftung, the Fonds der chemischen Industrie, and the Center for integrated Protein Science Munich, CiPSM. T.B. acknowledges funding from the Studienstiftung des deutschen Volkes. We thank Prof. Dr. Mohamed Marahiel and Alan Tanovic for providing recombinant SrfAC enzyme. We thank Kerstin Kurz for excellent technical assistance and Maximilian Pitscheider for help with recombinant expression.

Abstract

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A chemical proteomic strategy has been applied directly to bacterial proteomes, and β-lactones have been identified as important natural product derivatives with a high affinity to various enzyme classes (see picture). This approach may serve as a potent tool for the identification of novel antibacterial targets, the study of their function, and the definition of novel lead structures for the design of enzyme inhibitors.

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