PGK2 Human

PGK2 is a member of the phosphoglycerate kinase family and catalyzes the reversible conversion of 1,3-bisphosphoglycerate to 3-phosphoglycerate during glycolysis. This reaction is essential for the production of ATP, which is a critical energy source for various cellular processes . The enzyme’s activity is vital for sperm motility and male fertility, although it is not required for the completion of spermatogenesis .

The PGK2 gene is located on chromosome 6 and is expressed exclusively in the testis. The protein encoded by this gene has a molecular weight of approximately 44,664.93 Da and a theoretical isoelectric point (pI) of 8.74 . The gene was initially thought to be a pseudogene, but it was later discovered to encode a functional enzyme .

Mutations or deficiencies in the PGK2 gene can be associated with certain diseases, including Triosephosphate Isomerase Deficiency and Spastic Paraplegia 33, Autosomal Dominant . The enzyme’s role in glycolysis and energy production makes it a critical component in cellular metabolism, particularly in the context of reproductive health.

Recombinant PGK2 is produced using advanced protein expression technologies. This involves gene synthesis, protein codon optimization, and the use of various expression systems such as bacterial, yeast, baculovirus-insect, and mammalian systems. The recombinant protein is then purified and tested for activity .

PGK2 is a subject of extensive research due to its role in glycolysis and male fertility. Understanding its function and regulation can provide insights into metabolic disorders and potential therapeutic targets. Recombinant PGK2 is used in various biochemical assays and research studies to explore its enzymatic properties and potential applications in medicine .