UGP2 Human

UGP2 catalyzes the conversion of glucose-1-phosphate and uridine triphosphate (UTP) to UDP-glucose and pyrophosphate (PPi). This reaction is crucial for the formation of UDP-glucose, which serves as a glycosyl donor in the biosynthesis of glycogen and glycoproteins . The enzyme’s activity is dependent on the presence of magnesium ions (Mg2+), which act as cofactors in the reaction .

UDP-glucose is a central metabolite in the biosynthesis of glycogen, a storage form of glucose, and in the glycosylation of proteins and lipids. Glycosylation is a critical post-translational modification that affects protein folding, stability, and function. UGP2’s role in these processes underscores its importance in maintaining cellular homeostasis and energy balance .

Recent studies have highlighted the significance of UGP2 in cancer metabolism, particularly in pancreatic ductal adenocarcinoma (PDAC). UGP2 is upregulated in some cancers, and its expression is regulated by the Yes-associated protein 1 (YAP)-TEA domain transcription factor (TEAD) complex . Loss of UGP2 leads to decreased intracellular glycogen levels and defects in N-glycosylation targets, including the epidermal growth factor receptor (EGFR), which are crucial for cell growth and survival . These findings suggest that UGP2 could be a potential therapeutic target for cancer treatment.

Human recombinant UGP2 is produced using recombinant DNA technology, which involves inserting the human UGP2 gene into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the enzyme for research and therapeutic purposes. Recombinant UGP2 retains the same biochemical properties and functions as the native enzyme, making it a valuable tool for studying carbohydrate metabolism and developing potential treatments for metabolic disorders and cancers .