Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Photoaffinity labeling for evaluation of uridinyl analogs as specific inhibitors of rat liver microsomal UDP-glucuronosyltransferases
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2008, Carbohydrate ResearchCitation Excerpt :As surrogate of the diphosphate, we selected the oxycarbonylaminosulfonyl linker, a non-charged isostere of pyrophosphate, for three reasons: Both carbonyl and sulfonyl groups have been used as phosphate substitutes in several examples.11–13 The carbamate group is cleaved by glycosidases with the release of CO2;14 thereby in view of some similarity between glycosidases and glycosyltransferases, we guessed there was a reasonable chance that the carbamate group might also be substrate for glycosyltransferases.
Structure of UDP-glucuronosyltransferases in membranes
2005, Methods in EnzymologyCitation Excerpt :Specifically, the use of 5‐azido‐substituted nucleotide affinity analogs has resulted in substantial progress in the characterization of native UGTs (Drake and Elbein, 1992; Radominska and Drake, 1994; Rachmel et al., 1985). The identification of novel proteins, effective monitoring of UGT purification processes, and evaluation of the effects of pH, inhibitors, detergents, competing nucleotides, and proteolytic digestion on enzyme activity can be evaluated, as is described in several papers (Drake et al., 1989, 1991a,b; Radominska et al., 1994a,b,c). Photoaffinity labeling can generate the most important information when applied to the specific amino acid present in the active site of UGTs.
Natural and synthetic inhibitors of UDP-glucuronosyltransferase
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