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

被引：102

作者：

Peters, Wibke ^{[1
,2
]}

Willnow, Sophie ^{[1
]}

Duisken, Mike ^{[3
]}

Kleine, Henning ^{[2
]}

Macherey, Thomas ^{[1
]}

Duncan, Kelly E. ^{[4
]}

Litchfield, David W. ^{[4
]}

Luescher, Bernhard ^{[2
]}

Weinhold, Elmar ^{[1
]}

机构：

[1] Rhein Westfal TH Aachen, Inst Organ Chem, D-52056 Aachen, Germany

[2] Rhein Westfal TH Aachen, Inst Biochem & Mol Biol, Sch Med, D-52074 Aachen, Germany

[3] Leco Instruments GmbH, Monchengladbach, Germany

[4] Univ Western Ontario, Dept Biochem, Schulich Sch Med & Dent, London, ON, Canada

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2010年 / 49卷 / 30期

基金：

加拿大健康研究院;

关键词：

click chemistry; cofactors; epigenetics; proteins; transferases; LYSINE METHYLTRANSFERASE; H3K4; TRIMETHYLATION; TERMINAL ALKYNES; HISTONE H3R2; METHYLATION; COMPLEX; DNA; COFACTORS; TARGETS; AZIDES;

D O I：

10.1002/anie.201001240

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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-methioninebased cofactor was synthesized and used for the sitespecific functionalization of proteins with alkynes by methyltransferases (first step) and subsequent labeling through CuAAC click chemistry (second step; see scheme). (Figure Presented). © 2010 Wiley-VCH Verlag GmbH & Co.KGaA.

引用

页码：5170 / 5173

页数：4

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