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PKLR 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. 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 have been described: the R- and L-types. Note: This description may include information from UniProtKB.
Protein type: Carbohydrate Metabolism - glycolysis and gluconeogenesis; Carbohydrate Metabolism - pyruvate; EC; Kinase, other; Nucleotide Metabolism - purine
Chromosomal Location of Human Ortholog: 1q22
Cellular Component: cytoplasm; cytosol
Molecular Function: pyruvate kinase activity
Biological Process: cellular response to insulin stimulus; glycolysis
Disease: Adenosine Triphosphate, Elevated, Of Erythrocytes; Pyruvate Kinase Deficiency Of Red Cells
Reference #:  P30613 (UniProtKB)
Alt. Names/Synonyms: KPYR; PK1; PKL; PKLR; PKR; PKRL; Pyruvate kinase 1; pyruvate kinase isozyme R/L; Pyruvate kinase isozymes R/L; pyruvate kinase type L; pyruvate kinase, liver and blood cell; pyruvate kinase, liver and RBC; R-type/L-type pyruvate kinase; Red cell/liver pyruvate kinase; RPK
Gene Symbols: PKLR
Molecular weight: 61,830 Da
Basal Isoelectric point: 7.65  Predict pI for various phosphorylation states
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Protein Structure Not Found.
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