Structural Analysis of
ATP Analogues Compatible with
Kinase-Catalyzed Labeling
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Abstract
Kinase-catalyzed protein phosphorylation is an important
biochemical
process involved in cellular functions. We recently discovered that
kinases promiscuously accept γ-modified ATP analogues as cosubstrates
and used several ATP analogues as tools for studying protein phosphorylation.
Herein, we explore the structural requirements of γ-modified
ATP analogues for kinase compatibility. To understand the influence
of linker length and composition, a series of ATP analogues was synthesized,
and the efficiency of kinase-catalyzed labeling was determined by
quantitative mass spectrometry. This study on factors influencing
kinase cosubstrate promiscuity will enable design of ATP analogues
for a variety of kinase-catalyzed labeling reactions