PGK1 Human

PGK1 is encoded by the PGK1 gene located on the X chromosome. The gene is highly conserved across different species, indicating its essential role in cellular metabolism . The protein consists of 417 amino acids and has a molecular weight of approximately 44.5 kDa .

Apart from its primary role in glycolysis, PGK1 has been identified as a moonlighting protein, meaning it performs multiple mechanistically distinct functions. For instance, PGK1 acts as a cofactor for polymerase alpha, playing a role in DNA replication . Additionally, PGK1 is involved in angiogenesis, the process of forming new blood vessels, by reducing disulfide bonds in the serine protease plasmin, leading to the release of angiostatin, a tumor blood vessel inhibitor .

Deficiency in PGK1 can lead to a variety of clinical phenotypes, including hemolytic anemia and neurological impairments . The enzyme’s dysregulation has also been observed in numerous malignancies, making it a potential target for cancer therapy . For example, PGK1 is upregulated in non-small cell lung cancer (NSCLC) and is associated with poor prognosis . Inhibition of PGK1 has been shown to reduce NSCLC cell proliferation, migration, and invasion .

Human recombinant PGK1 is produced using recombinant DNA technology, which involves inserting the human PGK1 gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications, including studies on glycolysis, cancer metabolism, and enzyme kinetics .