ABSTRACT
This chapter considers the various advantages of using synthetic substrate peptides to study protein phosphatases, to review several specific examples of studies that have employed synthetic peptides. It suggests future directions and applications of synthetic peptides in the study of protein phosphatase structure, function, and regulation. The use of synthetic peptide substrates for work with protein phosphatases has a number of advantages compared to using protein substrates. Perhaps the most important overall advantage to using synthetic peptides as substrates is that they are chemically well-defined entities that can be obtained in highly purified form and in relatively large quantity. Synthetic peptides are ideally suited for characterizing the biochemical properties of protein phosphatases, as well as for developing enzyme-specific assays of phosphatase activity. Synthetic peptides based on the structure of the phosphorylation site of pyruvate kinase have been the most extensively used phosphopeptides for studying protein phosphatases.
