PKM: one of three rate-limiting enzymes in glycolysis. It catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule ATP and a pyruvate molecule, which is a central metabolic intermediate that can be used as a building block or oxidized further. Overexpressed in a variety of cancers. Interacts with thyroid hormone, and thus may mediate cellular metabolic effects induced by thyroid hormones. Binds Opa protein, a bacterial outer membrane protein involved in gonococcal adherence to and invasion of human cells, suggesting a role of this protein in bacterial pathogens is. There are several mammalian isozymes of pyruvate kinase encoded by different genes. The L type predominates in liver, and the M type in muscle and brain. Two alternatively spliced human isoforms of PKM2 have been reported.
Protein type: Carbohydrate Metabolism - glycolysis and gluconeogenesis; Carbohydrate Metabolism - pyruvate; EC 2.7.1.40; Kinase, other; Mitochondrial; Nucleotide Metabolism - purine
Chromosomal Location of Human Ortholog: 8q24
Cellular Component: cilium; cytoplasm; cytosol; extracellular matrix; mitochondrion; myelin sheath; nucleus; vesicle
Molecular Function: ADP binding; ATP binding; cadherin binding; identical protein binding; kinase activity; magnesium ion binding; potassium ion binding; protein binding; pyruvate kinase activity; RNA binding
Biological Process: ATP biosynthetic process; cellular response to insulin stimulus; glucose metabolic process; glycolytic process; liver development; organ regeneration; programmed cell death; protein homotetramerization; pyruvate biosynthetic process; response to gravity; response to hypoxia; response to insulin stimulus; response to muscle inactivity; response to nutrient; response to organic substance; skeletal muscle tissue regeneration
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