Biochemical and Biophysical Research Communications
The effect of N-linked glycosylation on the substrate preferences of UDP glucuronosyltransferases
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Cited by (24)
The UGTome: The expanding diversity of UDP glycosyltransferases and its impact on small molecule metabolism
2019, Pharmacology and TherapeuticsCitation Excerpt :Subsequently, endoglycosidase H digestions of purified and recombinant proteins demonstrated the presence of oligosaccharide chains attached to asparagine residues in UGT proteins (Green & Tephly, 1989; Mackenzie, 1990). The glycan chain was not essential for catalytic activity and appeared not to alter the substrate preferences of each UGT (Mackenzie, 1990). However, it may be important for correct folding and maintenance of fully-active enzymes, as described for UGT1A9 (Nakajima et al., 2010) and UGT2B7 (Girard-Bock, Benoit-Biancamano, Villeneuve, Desjardins, & Guillemette, 2016).
Characterization of human UGT2A3 expression using a prepared specific antibody against UGT2A3
2019, Drug Metabolism and PharmacokineticsCitation Excerpt :UGTs are membrane-bound enzymes associated with post-translational modifications through the ER. Some UGT isoforms are N-linked glycosylated on the ER membrane [26–30]. As shown in Fig. 2A, UGT2A3 also contains potential N-glycosylation sites.
Hepatic Drug Metabolism in Pediatric Patients
2017, Drug Metabolism in DiseasesThe effects of N-glycosylation on the glucuronidation of zidovudine and morphine by UGT2B7 expressed in HEK293 cells
2012, Drug Metabolism and PharmacokineticsN-Glycosylation plays a role in protein folding of human UGT1A9
2010, Biochemical PharmacologyCitation Excerpt :As for UGTs, it has been demonstrated that deglycosylation of the purified rabbit UGT1A6, UGT2B13, rat UGT1A6 and UGT2B2 proteins by endoglycosidase H (Endo H) did not decrease their enzyme activities [10]. Mackenzie [9] has reported that rat UGT2B1 and UGT2B2 are N-glycosylated and the treatment of COS cells expressing these UGTs with tunicamycin, which inhibits the first step of N-glycosylation, i.e., translocation of oligosaccharide core units to peptides, resulted in the production of less active enzymes. However, the unglycosylated proteins showed similar substrate specificity and protein stability as the native proteins.