3 years ago

Chemical Approaches to Investigate Labile Peptide and Protein Phosphorylation

Chemical Approaches to Investigate Labile Peptide and Protein Phosphorylation
Anett Hauser, Christian P. R. Hackenberger, Martin Penkert
Protein phosphorylation is by far the most abundant and most studied post-translational modification (PTM). For a long time, phosphate monoesters of serine (pSer), threonine (pThr), and tyrosine (pTyr) have been considered as the only relevant forms of phosphorylation in organisms. Recently, several research groups have dedicated their efforts to the investigation of other, less characterized phosphoamino acids as naturally occurring PTMs. Such apparent peculiar phosphorylations include the phosphoramidates of histidine (pHis), arginine (pArg), and lysine (pLys), the phosphorothioate of cysteine (pCys), and the anhydrides of pyrophosphorylated serine (ppSer) and threonine (ppThr). Almost all of these phosphorylated amino acids show higher lability under physiological conditions than those of phosphate monoesters. Furthermore, they are prone to hydrolysis under acidic and sometimes basic conditions as well as at elevated temperatures, which renders their synthetic accessibility and proteomic analysis particularly challenging.

Publisher URL: http://dx.doi.org/10.1021/acs.accounts.7b00170

DOI: 10.1021/acs.accounts.7b00170

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