41029-46-3Relevant articles and documents
A Selenium-Based Click AdoMet Analogue for Versatile Substrate Labeling with Wild-Type Protein Methyltransferases
Willnow, Sophie,Martin, Michael,Luescher, Bernhard,Weinhold, Elmar
, p. 1167 - 1173 (2012)
Protein methylation is catalyzed by S-adenosyl-L-methionine-dependent protein methyltransferases (MTases), and this posttranslational modification serves diverse cellular functions. Some MTases seem to exhibit broad substrate specificities and comprehensive methods for target profiling are needed. Here we report the synthesis of a new AdoMet analogue for enzymatic transfer of a small propargyl group and labeling of modified proteins through copper-catalyzed azide-alkyne cycloaddition (CuAAC). Replacement of sulfur by selenium strongly enhanced the stability of the progargylic cofactor, leading, in combination with better activation by the selenonium center, to higher enzymatic reactivity. A broad spectrum of wild-type protein MTases acting on lysine, arginine, and glutamine residues accept this cofactor and modified substrates can be efficiently labeled by CuAAC click chemistry.
Quaternization of Vinyl/Alkynyl Pyridine Enables Ultrafast Cysteine-Selective Protein Modification and Charge Modulation
Matos, Maria J.,Navo, Claudio D.,Hakala, Tuuli,Ferhati, Xhenti,Guerreiro, Ana,Hartmann, David,Bernardim, Barbara,Saar, Kadi L.,Compa?ón, Ismael,Corzana, Francisco,Knowles, Tuomas P. J.,Jiménez-Osés, Gonzalo,Bernardes, Gon?alo J. L.
, p. 6640 - 6644 (2019)
Quaternized vinyl- and alkynyl-pyridine reagents were shown to react in an ultrafast and selective manner with several cysteine-tagged proteins at near-stoichiometric quantities. We have demonstrated that this method can effectively create a homogenous an
Quaternized tellurium salt fog inhibiting agents for silver halide photography
-
, (2008/06/13)
-
