NP-M2tide

The phosphorylated form of this peptide, GGAVDDDYAQFANGG, was discovered through screening a peptide library for peptides that will bind to Pyruvate kinase M2 isoform (PKM2), which is found in fetal and cancer cells. PKM2 can be regulated by tyrosine kinase signaling pathways via a novel phosphotyrosine-binding ability. Binding of phosphotyrosine peptides to PKM2 catalyses the release of FBP and subsequent inhibition of enzymatic activity. Because proliferating cells require de novo fatty acid synthesis as well as DNA replication, one possible model is that regulation of PKM2 activity allows for a balance between ATP production and fatty acid/nucleic acid production. Alternatively, phosphotyrosine-based regulation of PKM2 enzymatic activity may provide a direct link between cell growth signals using tyrosine kinases and control of glycolytic metabolism. This peptide can be used as a control for the phosphorylated form of this peptide (BML-CA239).