Radiation inactivation analysis of microsomal UDP-glucuronosyltransferases catalysing mono-and diglucuronide formation of 3,6-dihydroxybenzo(a)pyrene and 3,6-dihydroxychrysene
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Hetero-oligomer formation of mouse UDP-glucuronosyltransferase (UGT) 2b1 and 1a1 results in the gain of glucuronidation activity towards morphine, an activity which is absent in homo-oligomers of either UGT
2020, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Although we used different ratios of Ugt1a1 and Ugt2b1, the optimal molecular ratio of the two UGTs for maximal morphine glucuronidation is unknown. As previous studies suggested that UGTs form dimers and tetramers [8,28], we prepared microsomes expressing Ugt1a1:Ugt2b1 in different ratios and compared levels of M-3-G generation (Fig. 3). Despite the different expression levels, there was no significant differences in CLint values (Table 2).
The UGTome: The expanding diversity of UDP glycosyltransferases and its impact on small molecule metabolism
2019, Pharmacology and TherapeuticsEvaluation of UGT protein interactions in human hepatocytes: Effect of siRNA down regulation of UGT1A9 and UGT2B7 on propofol glucuronidation in human hepatocytes
2013, Archives of Biochemistry and BiophysicsCitation Excerpt :Co-localization and protein–protein interactions between drug metabolizing enzymes allows concerted metabolism to occur more efficiently [13]. Several studies also suggest that the UGTs themselves dimerize and are functional as dimers in monoglucuronide formation or as tetramers in diglucuronide formation [14]. It is the highly variable, substrate binding N-terminus that has generally been implicated in these protein–protein interactions, though evidence exists that the C-terminus may also have a role [15,16].
Interactions between human UDP-glucuronosyltransferase (UGT) 2B7 and UGT1A enzymes
2010, Journal of Pharmaceutical Sciences