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Structural analysis of ATP analogues compatible with kinase-catalyzed labeling.

ABSTRACT: Kinase-catalyzed protein phosphorylation is an important biochemical process involved in cellular functions. We recently discovered that kinases promiscuously accept ?-modified ATP analogues as cosubstrates and used several ATP analogues as tools for studying protein phosphorylation. Herein, we explore the structural requirements of ?-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.

SUBMITTER: Suwal S

PROVIDER: S-EPMC3745010 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Structural analysis of ATP analogues compatible with kinase-catalyzed labeling.

Suwal Sujit S Senevirathne Chamara C Garre Satish S Pflum Mary Kay H MK

Bioconjugate chemistry 20121113 12

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 e ...[more]

PMID: 23116557

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