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Enzymatic Site‐Specific Functionalization of Protein Methyltransferase Substrates with Alkynes for Click Labeling
Author(s) -
Peters Wibke,
Willnow Sophie,
Duisken Mike,
Kleine Henning,
Macherey Thomas,
Duncan Kelly E.,
Litchfield David W.,
Lüscher Bernhard,
Weinhold Elmar
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201001240
Subject(s) - methyltransferase , click chemistry , methylation , surface modification , chemistry , methionine , protein methylation , enzyme , posttranslational modification , biochemistry , combinatorial chemistry , cofactor , stereochemistry , amino acid , dna
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).