PKM2 is a pyruvate kinase that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate to ADP, generating ATP and pyruvate. PKM2 plays a crucial role in cellular metabolism, specifically in glycolysis, where PKM2 catalyzes the conversion of phosphoenolpyruvate to pyruvate, generating adenosine triphosphate (ATP) in the process. This function is vital for energy production in cells, particularly in tissues with high metabolic demands, such as muscle and brain. PKM gene encodes two isoforms, M1 and M2, through alternative splicing, with both isoforms forming tetramers that are activated by fructose 1,6-bisphosphate. Notably, M2-type isoform has been shown to interact with Oct-4, a key transcription factor in stem cell biology, enhancing transcriptional activity and thereby influencing cellular differentiation and proliferation.