
-   Size: 574 amino acids
-   Molecular mass: 61830 Da
-   Protein Accession: P30613
-   Family: Belongs to the pyruvate kinase family
-   Domains: Pyr_Knase, Pyrv/PenolPyrv_Kinase-like_dom, Pyrv_Kinase-like_dom_sf, Pyrv_Knase-like_insert_dom_sf, Pyrv_Knase_AS, Pyrv_Knase_brl, Pyrv_Knase_C, Pyrv_Knase_C_sf, Pyrv_Knase_insert_dom_sf
-   The PK-LR gene, associated with congenital haemolytic anemia, was studied in 10 Indian patients, revealing nine different mutations, two of which were novel, and the structural implications of these amino acid substitutions were correlated with the observed clinical phenotypes [PMID: 23770304].
-   Mutational analyses of the human liver pyruvate kinase (PKLR) protein suggest that mutations within the allosteric amino-acid-binding site can modify the allosteric coupling constant, supporting a speculative mechanism for how alanine allosterically modifies PKLR's affinity for its substrate, phosphoenolpyruvate [PMID: 28459139].
-   Site-directed mutagenesis of the PKLR gene promoter region revealed the presence of a putative regulatory element (PKR-RE1) whose core binding motif, CTCTG, is located between nt-87 and nt-83. This element mediates the effects of factors necessary for regulation of pyruvate kinase gene expression during red cell differentiation and maturation [PMID: 12393511].
