title: 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 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.
authors.affiliation: Department of Chemistry, Wayne State University, Detroit, MI 48202, USA.
authors.forename: Sujit
authors.initials: S
authors.lastname: Suwal
authors.forename: Chamara
authors.initials: C
authors.lastname: Senevirathne
authors.forename: Satish
authors.initials: S
authors.lastname: Garre
authors.forename: Mary Kay H
authors.initials: MK
authors.lastname: Pflum
mesh_terms: D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000737:chemistry*; D000588:Amines / Q000737:chemistry*; D001665:Binding Sites; D002384:Catalysis; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry*; D007700:Kinetics; D013058:Mass Spectrometry; D062105:Molecular Docking Simulation; D010455:Peptides / Q000737:chemistry*; D010766:Phosphorylation; D013194:Staining and Labeling / Q000379:methods*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D000588:Amines; D010455:Peptides; D000255:Adenosine Triphosphate; D017868:Cyclic AMP-Dependent Protein Kinases