Enzymatic Site‐Specific Functionalization of Protein Methyltransferase Substrates with Alkynes for Click Labeling | Zendy

Peters Wibke | Zendy; Willnow Sophie | Zendy; Duisken Mike | Zendy; Kleine Henning | Zendy; Macherey Thomas | Zendy; Duncan Kelly E. | Zendy; Litchfield David W. | Zendy; Lüscher Bernhard | Zendy; Weinhold Elmar | Zendy

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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).

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