19914-41-1Relevant articles and documents
Fluorogenic peptide substrates for serine and threonine phosphatases
Xue, Fengtian,Seto, Christopher T.
supporting information; experimental part, p. 1936 - 1939 (2010/07/06)
Figure presented A new fluorescent assay for Ser/Thr protein phosphatases has been developed. Hydrolysis of a phosphoSer residue liberates the Ser hydroxyl group, which induces a cyclization reaction on the N-terminal carbamate and releases a fluorescent reporter. Sequence selectivity is observed using several peptide substrates against alkaline phosphatase (ALP), bacteriophage protein phosphatase (-PPase), and vaccinia H1 related phosphatase (VHR). These studies suggest that the assay could be a useful tool for profiling the substrate specificities of medicinally important phosphatases.