UDP-glucuronate decarboxylase 1 (UXS1)

UDP-glucuronate decarboxylase 1 (UXS1) is an enzyme residing primarily in the Golgi apparatus that catalyzes the decarboxylation of UDP-glucuronic acid to UDP-xylose, the first sugar in the glycosaminoglycan (GAG) linker region of proteoglycans[1][2][6]. This reaction is critical for the biosynthesis of glycosaminoglycans, which are essential for the structure and function of the extracellular matrix and cell surface proteoglycans[2][5]. The enzyme is encoded by the UXS1 gene and belongs to the short chain dehydrogenase/reductase (SDR) family[1][2]. UXS1 activity is vital for normal development, and its dysfunction results in severe genetic syndromes (linkeropathies) and may be exploited as a metabolic vulnerability in cancer cells due to the toxicity associated with UDP-glucuronic acid accumulation[4][5]. There are currently no widely reported drug modulators or established biomarkers for this target.

Other names

UDP-glucuronic acid decarboxylase 1UGDUXS-1hUXShUXS1FLJ23591SDR6E1UNQ2538/PRO6079short chain dehydrogenase/reductase family 6E member 12

Enzyme inhibition (drugs or genetic knockout causing accumulation of UDP-glucuronic acid, leading to Golgi dysfunction and cell death in cancer cells)[4]