PKLR Antibody – Rabbit Polyclonal

The protein encoded by this gene is a pyruvate kinase that catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP, which is the rate-limiting step of glycolysis. Defects in this enzyme, due to gene mutations or genetic variations, are the common cause of chronic hereditary nonspherocytic hemolytic anemia (CNSHA or HNSHA). Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

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.

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

Chromosomal Location of Human Ortholog: 1q21

Cellular Component: cytosol

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

Biological Process: pyruvate biosynthetic process; response to cAMP; glycolysis; response to lithium ion; positive regulation of cellular metabolic process; glucose metabolic process; pathogenesis; response to other organism; endocrine pancreas development; response to ATP; cellular response to insulin stimulus; response to heat; ATP biosynthetic process; carbohydrate metabolic process; energy reserve metabolic process; response to glucose stimulus; response to hypoxia; phosphorylation; response to nutrient

Disease: Adenosine Triphosphate, Elevated, Of Erythrocytes; Pyruvate Kinase Deficiency Of Red Cells