The comprehensive identification of ATP-binding proteins like the important class of kinases and the dynamic analysis of nucleotide-protein interactions at the proteomic scale are fundamental for understanding better the regulatory mechanisms of nucleotide-binding proteins.
ATP binding activities as well as specific binding sites of proteins can be detected globally in any biological sample or tissue from any species by using Biotin/Desthiobiotin-conjugated acyl-ATP probes (AcATP)[2-6].
(Scheme adapted from Xiao et al.)
• AcATP binds to the pocket of ATP binding proteins and places the acyl group in close proximity to conserved lysine residues.
• Nucleophilic attack by the amino group of the lysine at the AcATP probe.
• Amide bond formation resulting in a covalent attachment of the acyl reporter of the AcATP probe on the lysine and a concomitant release of ATP.
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 Manning et al. (2002) The protein kinase complement of the human genome. Science 298:1912.
 Villamor et al. (2013) Profiling protein kinases and other ATP binding proteins in Arabidopsis using Acyl-ATP probes. Molecular & Cellular Proteomics 12 (9):2481.
 Xiao et al. (2013) Proteome-wide discovery and characterizations of nucleotide-binding proteins with affinity-labeled chemical probes. Anal. Chem. 85 (6):3198.
 Okerberg et al. (2019) Chemoproteomics using nucleotide acyl phosphates reveals an ATP binding site at the dimer interface of procaspase-6. Biochemistry 58 (52):5320.
 Nordin et al. (2015) ATP acyl phosphate reactivity reveals native conformations of Hsp90 paralogs and inhibitor target engagement. Biochemistry 54 (19):3024.
 Adachi et al. (2014) Proteome-wide discovery of unknown ATP-binding proteins and kinase inhibitor target proteins using an ATP probe. J. Proteome Res. 13 (12):5461.