ATP-polyamine-biotin is the first cell-permeable ATP analogue and an efficient kinase cosubstrate. It promotes biotin labeling of kinase substrates in live cells. In in vitro studies, when incubated with PKA kinase and full-length myelin basic protein (MBP) substrate, biotinylation was observed only in the presence of the kinase. The biotinylation of MBP was absent without this compound, in the presence of the kinase inhibitor staurosporine, or when incubated with acid, which causes cleavage of the phosphoramidate bond. A biotinylated kemptide product was observed exclusively with this cosubstrate.
- First cell-permeable ATP analogue
- Efficient kinase cosubstrate
- Promotes biotin labeling of kinase substrates in live cells