| This gene encodes a protein involved in glycolysis. The encoded protein is a pyruvate kinase that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate to ADP, generating ATP and pyruvate. This protein has been shown to interact with thyroid hormone and may mediate cellular metabolic effects induced by thyroid hormones. This protein has been found to bind 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 pathogenesis. Several alternatively spliced transcript variants encoding a few distinct isoforms have been reported. [provided by RefSeq, May 2011],catalytic activity:ATP + pyruvate = ADP + phosphoenolpyruvate.,cofactor:Divalent metal cations.,cofactor:Magnesium.,cofactor:Potassium.,enzyme regulation:Isoform M2 is allosterically activated by D-fructose 1,6-biphosphate (FBP). Inhibited by oxalate and 3,3,5-triiodo-L-thyronine (T3).,function:Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP.,miscellaneous:There are 4 isozymes of pyruvate kinase in mammals: L, R, M1 and M2. L type is major isozyme in the liver, R is found in red cells, M1 is the main form in muscle, heart and brain, and M2 is found in early fetal tissues as well as in most cancer cells.,online information:Pyruvate kinase entry,pathway:Carbohydrate degradation, glycolysis, pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.,PTM:Phosphorylated upon DNA damage, probably by ATM or ATR.,similarity:Belongs to the pyruvate kinase family.,subunit:Monomer and homotetramer. Exists as a monomer in the absence of FBP, and reversibly associates to form a homotetramer in the presence of FBP. The monomeric form binds T3. Tetramer formation induces pyruvate kinase activity. Interacts with HERC1., |
