PYRUVATE KINASE (PKM) RABBIT Active Protein

PKM2: 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: Kinase, other; Carbohydrate Metabolism - pyruvate; Carbohydrate Metabolism - glycolysis and gluconeogenesis; Nucleotide Metabolism - purine; EC 2.7.1.40; Mitochondrial

Cellular Component: extracellular matrix; mitochondrion; cytoplasm; plasma membrane; nucleus; vesicle; myelin sheath; cilium

Molecular Function: potassium ion binding; protein binding; magnesium ion binding; ADP binding; pyruvate kinase activity; ATP binding

Biological Process: pyruvate biosynthetic process; response to gravity; organ regeneration; glycolysis; programmed cell death; glucose metabolic process; skeletal muscle regeneration; liver development; response to insulin stimulus; response to organic substance; ATP biosynthetic process; response to hypoxia; phosphorylation; response to nutrient; response to muscle inactivity