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The UDP-glucuronosyltransferases as oligomeric enzymes.
TLDR
This article reviews, sometimes critically, most of the available studies about the oligomeric state of the UDP-glucuronosyltransferases and concludes that the UGTs are oligomersic enzymes, and discusses hetero-oligomerization among U GTs and its possible implications for the structure, function and substrate specificity of the enzymes. Expand
Expression and Characterization of Recombinant Human UDP-glucuronosyltransferases (UGTs)
TLDR
Eight human liver UDP-glucuronosyltransferases were expressed in baculovirus-infected insect cells as fusion proteins carrying a short C-terminal extension that ends with 6 histidine residues (His tag), and His-tagged UGT1A9 was purified by immobilized metal-chelating chromatography (IMAC). Expand
KINETIC CHARACTERIZATION OF THE 1A SUBFAMILY OF RECOMBINANT HUMAN UDP-GLUCURONOSYLTRANSFERASES
The initial glucuronidation rates were determined for eight recombinant human UDP-glucuronosyltransferases (UGTs) of the 1A subfamily, and the bisubstrate kinetics and inhibition patterns wereExpand
Glucuronidation of anabolic androgenic steroids by recombinant human UDP-glucuronosyltransferases.
TLDR
The high activity of UGT1A8 and 1A10 toward some of the substrates indicates that extrahepatic enzymes might play a role in the metabolism of anabolic androgenic steroids. Expand
Interactions with other human UDP-glucuronosyltransferases attenuate the consequences of the Y485D mutation on the activity and substrate affinity of UGT1A6
TLDR
Hetero-oligomerization may play an important role in UDP-glucuronosyltransferases activity and this mutation, the Y486D mutant of UGT1A1, often causes hyperbilirubinaemia. Expand
The Human UDP-Glucuronosyltransferase: Identification of Key Residues within the Nucleotide-Sugar Binding Site
TLDR
The combined results of activity determinations, kinetic analyses, and modeling strongly suggest that His371 and Glu379 are directly involved in UDPGA binding but are not the general acid or general base. Expand
Mutation analysis in UGT1A9 suggests a relationship between substrate and catalytic residues in UDP-glucuronosyltransferases.
TLDR
This work investigates the role of H37, D143 and D148 in UGT1A9 by site-directed mutagenesis, activity and kinetic measurements with several substrates, and suggests that H37 is not critical in N-glucuronidation, but is so in O- GlcA. Expand
UDP-Glucuronosyltransferases in Conjugation of 5α- and 5β-Androstane Steroids
TLDR
The results shed new light on the substrate selectivity of individual UGTs in steroid glucuronidation and bear implications for doping analyses and its dependence of genetic polymorphism. Expand
Comparison of electrospray, atmospheric pressure chemical ionization, and atmospheric pressure photoionization in the identification of apomorphine, dobutamine, and entacapone phase II metabolites in
TLDR
Identification and comparison of conjugates formed from the current model drugs were successfully analyzed in different biological specimens of common interest to biomedical research and a fairly good relation was obtained between the data from in vivo and in vitro models of drug metabolism. Expand
Glucuronidation of oxidized fatty acids and prostaglandins B1 and E2 by human hepatic and recombinant UDP-glucuronosyltransferases Published, JLR Papers in Press, July 1, 2004. DOI
TLDR
Results indicate that glucuronidation may play a significant role in modulation of the availability of these fatty acid derivatives for cellular processes and a novel metabolic pathway for HETEs and PGs and the role of UGT1A isoforms in this process is demonstrated. Expand
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