UGDH + product
UGDH + product: Human UDP-glucose dehydrogenase (in complex with product)
PDB Code: 2QG4
UDP glucuronic acid is an essential metabolite required for the synthesis of extracellular matrix components (such as glycosaminoglycans involving hyaluronan, chondroitin sulfate, and heparan sulfate). A further important role is its role in the esterification of lipophilic endogenous (e.g. steroids) or xenobiotic compounds, thus forming excretable products.
The enzyme UDP-glucose dehydrogenase (UGDH) produces in a NAD+ dependent reaction UDP glucuronic acid from UDP-glucose, which then serves as substrate for UDP-glucuronyltransferases, resulting in the multiple metabolites described above.
The enzyme is expressed in many gastrointestinal tissues with highest levels observed in the liver; and expression of the enzyme is regulated by several proinflammatory cytokines, growth factors such as transforming growth factor beta or IL-beta, by androgens and xenobiotics like eugenol and rifampicin.
UGDH is a potential therapeutic target for the treatment of cancer as inhibition of hyaluronan synthesis has been shown to reduce tumor angiogenesis and thereby restrict in vivo growth of human prostate tumors. Furthermore UGDH also plays an important role in the control of sex steroid inactivation via glucuronidation in breast cancer cells.
The structure of human UGDH was solved in an unproductive substrate complex with NADH and UDP-glucose and as a product complex of NAD+ and UDP glucuronate. The structures reveal a hexameric arrangement, composed of a trimer of dimers.
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