Substrate specificity of the human UDP-glucuronosyltransferase UGT2B4 and UGT2B7
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چکیده
منابع مشابه
Short Communication Prevalence of Polymorphisms in the Human UDP-Glucuronosyltransferase 2B Family: UGT2B4(DE), UGT2B7(HY), and UGT2B15(DY)
UDP-glucuronosyltransferases (UGTs) of the UGT2B family conjugate steroid hormones as well as bile acids and xenobiotics. UGT2Bs are expressed in numerous human tissues, such as skin, breast, prostate, adipose, and intestine and are hypothesized to modulate steroid metabolism and excretion. Polymorphisms have been identified that may modify substrate specificities or enzyme activities of UGT2B ...
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The purpose of this work was to identify human UDP-glucuronosyltransferases (UGTs) capable of glucuronidating dopamine. Using a sensitive liquid chromatography-tandem mass spectrometry method, we screened all 19 known human UGTs and found that only one enzyme, UGT1A10, catalyzed dopamine glucuronidation at substantial rates, yielding both dopamine-4-O-glucuronide (37.1 pmol/min/mg) and dopamine...
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A rat kidney phenol UDP-glucuronosyltransferase cDNA was used to isolate a human liver phenol UDP-glucuronosyltransferase cDNA by screening of a human liver cDNA library in the expression vector lambda gt11. The 2.4-kilobase cDNA contained an open reading frame of 1593 base pairs coding for a protein of 531 residues. The human liver cDNA was subcloned into the vector pKCRH2. Transfection of thi...
متن کاملInvestigation of the substrate specificity of a cloned expressed human bilirubin UDP-glucuronosyltransferase: UDP-sugar specificity and involvement in steroid and xenobiotic glucuronidation.
A cloned human bilirubin UDP-glucuronosyltransferase (UGT) stably expressed in Chinese hamster V79 cells was used to assess the substrate specificity of the enzyme. The catalytic potential (Vmax/Km(bilirubin) of the enzyme with UDP-glucuronic acid (UDPGA) was 2-fold and 10-fold greater than that for UDP-xylose and UDP-glucose respectively. The formation of bilirubin mono- and di-conjugates was ...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2007
ISSN: 1742-464X
DOI: 10.1111/j.1742-4658.2007.05670.x