The generality of kinase-catalyzed biotinylation
| Autor: | Ahmed E. Fouda, D. Maheeka Embogama, Chamara Senevirathne, Mary Kay H. Pflum, Thilani A. Anthony |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Cell signaling Clinical Biochemistry Biotin Pharmaceutical Science 010402 general chemistry 01 natural sciences Biochemistry Article 03 medical and health sciences chemistry.chemical_compound Drug Discovery Humans Biotinylation Kinome Protein phosphorylation Phosphorylation Molecular Biology Chemistry Kinase Organic Chemistry 0104 chemical sciences Molecular Docking Simulation Kinetics 030104 developmental biology Phosphoprotein Molecular Medicine Protein Kinases |
| Zdroj: | Bioorganic & Medicinal Chemistry. 24:12-19 |
| ISSN: | 0968-0896 |
| DOI: | 10.1016/j.bmc.2015.11.029 |
| Popis: | Kinase-catalyzed protein phosphorylation is involved in a wide variety of cellular events. Development of methods to monitor phosphoproteins in normal and diseased states is critical to fully characterize cell signalling. Towards phosphoprotein analysis tools, our lab reported kinase-catalyzed labeling where γ-phosphate modified ATP analogs are utilized by kinases to label peptides or protein substrates with a functional tag. In particular, the ATP-biotin analog was developed for kinase-catalyzed biotinylation. However, kinase-catalyzed labeling has been tested rigorously with only a few kinases, preventing use of ATP-biotin as a general tool. Here, biotinylation experiments, gel or HPLC-based quantification, and kinetic measurements indicated that twenty-five kinases throughout the kinome tree accepted ATP-biotin as a cosubstrate. With this rigorous characterization of ATP-biotin compatibility, kinase-catalyzed labeling is now immediately useful for studying phosphoproteins and characterizing the role of phosphorylation in various biological events. |
| Databáze: | OpenAIRE |
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