PKM, EnkiLife, AMRe16219

Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect. Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed: 15996096, PubMed: 1854723). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (PubMed: 15996096, PubMed: 1854723). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed: 15996096, PubMed: 1854723). In addition to its role in glycolysis, also regulates transcription (PubMed: 18191611, PubMed: 21620138). Stimulates POU5F1-mediated transcriptional activation (PubMed: 18191611). Promotes in a STAT1-dependent manner, the expression of the immune checkpoint protein CD274 in ARNTL/BMAL1-deficient macrophages (By similarity). Also acts as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity: associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs (By similarity). Plays a general role in caspase independent cell death of tumor cells (PubMed: 17308100).