Abstract
Current interests in biochemical transformations based on protein kinase-catalyzed phosphorylations drive the identification and characterization of biological targets and potential inhibitors of protein kinase activity. A simple transfer of a phosphate group from adenosine triphosphate (ATP) to the Ser/Thr/Tyr residues of target proteins drives cellular processes, including cell expression, growth, and death. Currently, three major experimental approaches towards kinome analysis are available (a) genetic engineering of protein kinases, (b) modifications of target substrates, and (c) derivatization of ATP co-substrate. Each approach offers advantages but also has disadvantages, which are discussed in this perspective, alongside with a rationale for designing and developing biological tools for kinome study.
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