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: EC 188.8.131.52; Nucleotide Metabolism - purine; Kinase, other; Carbohydrate Metabolism - glycolysis and gluconeogenesis; Carbohydrate Metabolism - pyruvate
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; response to glucose stimulus; response to hypoxia; energy reserve metabolic process; phosphorylation; response to nutrient
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.