Recognition of proximally phosphorylated tyrosine residues and continuous analysis of phosphatase activity using a stable europium complex Sarah Hewitt Roanna Liu Stephen Butler 2134/28343 https://repository.lboro.ac.uk/articles/journal_contribution/Recognition_of_proximally_phosphorylated_tyrosine_residues_and_continuous_analysis_of_phosphatase_activity_using_a_stable_europium_complex/9389699 The recognition of proteins and their post-translational modifications using synthetic molecules is an active area of research. A common post-translational modification is the phosphorylation of serine, threonine or tyrosine residues. The phosphorylation of proximal tyrosine residues occurs in over 1000 proteins in the human proteome, including in disease-related proteins, so the recognition of this motif is of particular interest. We have developed a luminescent europium(III) complex, [Eu.1] + , capable of the discrimination of proximally phosphorylated tyrosine residues, from analogous mono- and non-phosphorylated tyrosine residues, more distantly-related phosphotyrosine residues and over proximally phosphorylated serine and threonine residues. [Eu.1] + was used to continuously monitor the phosphatase catalysed dephosphorylation of a peptide containing proximally phosphorylated tyrosine residues. 2018-02-01 12:13:36 Anion sensing Luminescence Europium Phosphorylation Enzyme assay Chemical Sciences not elsewhere classified