Pyrophosphorylation via selective phosphoprotein derivatization.

ABSTRACT: An important step in elucidating the function of protein post-translational modifications (PTMs) is gaining access to site-specifically modified, homogeneous samples for biochemical characterization. Protein pyrophosphorylation is a poorly characterized PTM, and here a chemical approach to obtain pyrophosphoproteins is reported. Photo-labile phosphorimidazolide reagents were developed for selective pyrophosphorylation, affinity-capture, and release of pyrophosphoproteins. Kinetic analysis of the reaction revealed rate constants between 9.2 × 10^-3 to 0.58 M^-1 s^-1, as well as a striking proclivity of the phosphorimidazolides to preferentially react with phosphate monoesters over other nucleophilic side chains. Besides enabling the characterization of pyrophos

SUBMITTER: Marmelstein AM 

PROVIDER: S-EPMC6050540 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature