PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17636046-2 2007 UGT1A3 glucuronidates the planar phenols 1-naphthol (1-NP) and 4-methylumbelliferone (4-MU), whereas UGT1A4 converts the tertiary amines lamotrigine (LTG) and trifluoperazine (TFP) to quaternary ammonium glucuronides. Amines 130-136 UDP glucuronosyltransferase family 1 member A3 Homo sapiens 0-6 17636046-11 2007 Thus, residues 36 and 40 of UGT1A3 and UGT1A4 are pivotal for the respective selectivities of these enzymes toward planar phenols and tertiary amines, although other regions of the proteins influence binding affinity and/or turnover. Amines 143-149 UDP glucuronosyltransferase family 1 member A3 Homo sapiens 28-34 9616184-0 1998 Glucuronidation of amines and other xenobiotics catalyzed by expressed human UDP-glucuronosyltransferase 1A3. Amines 19-25 UDP glucuronosyltransferase family 1 member A3 Homo sapiens 77-108 9616184-4 1998 We show that human UGT1A3, transiently expressed in human embryonic kidney 293 cells, also catalyzes the N-glucuronidation of primary, secondary, and tertiary amine substrates, such as 4-aminobiphenyl, diphenylamine, and cyproheptadine. Amines 159-164 UDP glucuronosyltransferase family 1 member A3 Homo sapiens 19-25 10901693-3 2000 Two UDP-glucuronosyltransferases (UGTs) present in human liver, UGT1A4 and UGT1A3, were previously shown to catalyze tertiary amine N-glucuronidation when expressed in HK293 cells. Amines 126-131 UDP glucuronosyltransferase family 1 member A3 Homo sapiens 75-81 10901693-9 2000 The results suggest that UGT1A4 and UGT1A3 catalyze high-K(M) N-glucuronidation of tertiary amine drugs, whereas the low-K(M) reaction requires either an alternative enzyme or a special conformation of UGT1A4 or UGT1A3 that can be attained in liver microsomes, but not in HK293 cell membranes. Amines 92-97 UDP glucuronosyltransferase family 1 member A3 Homo sapiens 36-42 10901693-9 2000 The results suggest that UGT1A4 and UGT1A3 catalyze high-K(M) N-glucuronidation of tertiary amine drugs, whereas the low-K(M) reaction requires either an alternative enzyme or a special conformation of UGT1A4 or UGT1A3 that can be attained in liver microsomes, but not in HK293 cell membranes. Amines 92-97 UDP glucuronosyltransferase family 1 member A3 Homo sapiens 212-218 9616184-5 1998 In contrast to expressed human UGT1A4, which catalyzes the glucuronidation of amines with high efficiency, glucuronidation of amines catalyzed by UGT1A3 exhibited low efficiency, suggesting that UGT1A3 makes only a limited contribution to the metabolic elimination of these compounds. Amines 126-132 UDP glucuronosyltransferase family 1 member A3 Homo sapiens 146-152 9616184-5 1998 In contrast to expressed human UGT1A4, which catalyzes the glucuronidation of amines with high efficiency, glucuronidation of amines catalyzed by UGT1A3 exhibited low efficiency, suggesting that UGT1A3 makes only a limited contribution to the metabolic elimination of these compounds. Amines 126-132 UDP glucuronosyltransferase family 1 member A3 Homo sapiens 195-201 9616184-7 1998 In addition to amines, expressed human UGT1A3 catalyzed the glucuronidation of opioids (e.g. morphine and buprenorphine), coumarins, flavonoids (e.g. naringenin and quercetin), anthraquinones, and small phenolic compounds (e.g. 4-nitrophenol). Amines 15-21 UDP glucuronosyltransferase family 1 member A3 Homo sapiens 39-45