Enzymatic Site-Specific Functionalization of Protein Methyltransferase Substrates with Alkynes for Click Labeling

Authors

Wibke Peters, RWTH Aachen University, Aachen, Germany
Sophie Willnow, RWTH Aachen University, Aachen, Germany
Mike Duisken, Leco Instruments GmbH, Mönchengladbach, Germany
Henning Kleine, RWTH Aachen University, Aachen, Germany
Thomas Macherey, RWTH Aachen University, Aachen, Germany
Kelly E. Duncan, The University of Western Ontario
David W. Litchfield, The University of Western OntarioFollow
Bernhard Lüscher, RWTH Aachen University, Aachen, Germany
Elmar Weinhold, RWTH Aachen University, Aachen, Germany

Document Type

Article

Publication Date

6-22-2010

Journal

Angewandte Chemie International Edition

Volume

49

Issue

30

First Page

5170

Last Page

5173

URL with Digital Object Identifier

http://dx.doi.org/10.1002/anie.201001240

Abstract

Pass and click: Protein methylation is an important posttranslational modification. Because the methyl group is a poor reporter group, new methods are needed to analyze methyltransferase substrates. A S-adenosyl-L-methionine-based cofactor was synthesized and used for the site-specific functionalization of proteins with alkynes by methyltransferases (first step) and subsequent labeling through CuAAC click chemistry (second step; see scheme).