Introduction. Enzymes of the human uridine diphosphate (UDP)-glycosyltransferase (UGT) superfamily catalyse the covalent addition of the sugar moiety from a UDP-sugar cofactor to relatively low molecular weight lipophilic substrates. UGT2B7 can utilise both UDP-glucuronic acid (UDP-GlcUA) and UDP-glucose (UDP-Glc) as cofactors. However, glucuronidation is the preferred metabolic pathway. Currently, it is unclear which residues in the UGT2B7 cofactor binding domain are responsible for the preferential binding of UDP-GlcUA.
|Number of pages||1|
|Publication status||Published - 2020|
- uridine diphosphate