Pyruvate Kinase M2
PKM2 (pyruvate kinase muscle isoform 2) is an isoform of pyruvate kinase (PK; ATP, pyruvate 2-O-phosphotranferase; EC 184.108.40.206), a terminal glycolytic enzyme that catalyzes an irreversible, rate-limiting transphosphorylation reaction between phosphoenolpyruvate (PEP) and adenosine diphosphate (ADP) to generate pyruvate and ATP, accounting for net glycolytic energy (ATP) generation (Mazurek 2011). Consumption of pyruvate in a number of pathways places this enzyme at a crucial metabolic intersection. PK is ubiquitously present in simple to complex organisms. In organisms where PK is absent, its function is fulfilled by another homologue, pyruvate phosphate dikinase (PPDK) (Saavedra-Lira et al. 1998). In most bacteria and lower eukaryotes, only one form of PK is found, although many bacteria have two isozymes. In plants, PK exists in the form of cytoplasmic and plastid isoforms, and in...
- Iqbal MA, Siddiqui FA, Chaman N, Gupta V, Kumar B, Gopinath P, et al. Missense mutations in pyruvate kinase M2 promote cancer metabolism, oxidative endurance, anchorage independence, and tumor growth in a dominant negative manner. J Biol Chem. 2014b;289(12):8098–105.PubMedPubMedCentralCrossRefGoogle Scholar
- Palsson-McDermott EM, Curtis AM, Goel G, Lauterbach MA, Sheedy FJ, Gleeson LE, et al. Pyruvate kinase M2 regulates Hif-1alpha activity and IL-1beta induction and is a critical determinant of the warburg effect in LPS-activated macrophages. Cell Metab. 2015;21(1):65–80.PubMedPubMedCentralCrossRefGoogle Scholar