| Name | UGT1 |
|---|---|
| Synonyms | GNT1; UGT; UGT 1; UGT1; GNT1; UGT1A; UGT1A@ |
| Name | 1-naphthol |
|---|---|
| CAS | 1-naphthalenol |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 17686537 | Leaver MJ, Wright J, Hodgson P, Boukouvala E, George SG: Piscine UDP-glucuronosyltransferase 1B. Aquat Toxicol. 2007 Oct 15;84(3):356-65. Epub 2007 Jul 1. The deduced amino acid sequences share greater similarity with mammalian UGT1 family genes than UGT2 genes (44-47% and 39-40% amino acid identity, respectively) and have been designated UGT1B. Expression of a cDNA for plaice UGT1B in cos7 cells resulted in higher 1-naphthol conjugation in cell homogenates compared to steroid conjugation, whilst and bile acid conjugation were undetectable. |
4(0,0,0,4) | Details |
| 15802387 | Luukkanen L, Taskinen J, Kurkela M, Kostiainen R, Hirvonen J, Finel M: Kinetic characterization of the 1A subfamily of recombinant human UDP-glucuronosyltransferases. Drug Metab Dispos. 2005 Jul;33(7):1017-26. Epub 2005 Mar 31. The glucuronidation of entacapone by UGT1A9 was inhibited by 1-naphthol in a competitive fashion, with respect to entacapone, and an uncompetitive fashion, with respect to UDP- (UDPGA). Despite the identical primary structure of the C-terminal halves of the UGT1A isoforms, there were marked differences in the respective K (m) values for UDPGA, ranging from 52 microM for UGT1A6 to 1256 microM for UGT1A8. |
3(0,0,0,3) | Details |
| 19487247 | Kerdpin O, Mackenzie PI, Bowalgaha K, Finel M, Miners JO: Influence of N-terminal domain and residues on the substrate selectivities of human UDP-glucuronosyltransferase 1A1, 1A6, 1A9, 2B7, and 2B10. Drug Metab Dispos. 2009 Sep;37(9):1948-55. Epub 2009 Jun 1. An N-terminal domain [corresponding to position 39 of UDP-glucuronosyltransferase (UGT) 1A1] is conserved in all UGT1A and UGT2B subfamily proteins except UGT1A4 (Pro-40) and UGT2B10 -34). |
2(0,0,0,2) | Details |
| 18004206 | Udomuksorn W, Elliot DJ, Lewis BC, Mackenzie PI, Yoovathaworn K, Miners JO: Influence of mutations associated with Gilbert and Crigler-Najjar type II syndromes on the glucuronidation kinetics of and other UDP-glucuronosyltransferase 1A substrates. Pharmacogenet Genomics. 2007 Dec;17(12):1017-29. This work compared the effects of (a) the individual UGT1A1 mutations on the glucuronidation kinetics 4-methylumbelliferone (4MU) and 1-naphthol (1NP), and (b) the Y486 mutation, which occurs in the conserved carboxyl terminal domain of UGT1A enzymes, on 4MU, 1NP and glucuronidation by UGT1A3, UGT1A6 and UGT1A10. |
2(0,0,0,2) | Details |
| 12051676 | Dean B, Chang S, Stevens J, Thomas PE, King C: Isolation and characterization of a UDP-glucuronosyltransferase (UGT1A01) cloned from female rhesus monkey. Arch Biochem Biophys. 2002 Jun 15;402(2):289-95. Nucleotide sequence comparison of rhesus UGT1A01 to other rhesus UGT1A isoforms detected a single-transition mutation at nucleotide 1520 (T--> C), resulting in a neutral F to S substitution at position 507. Catalytic activity of UGT1A01 was determined with 7--4-(trifluoromethyl)- and more specific human UGT1A1 substrates (1-naphthol, 17 alpha-ethinylestradiol, and |
2(0,0,0,2) | Details |
| 18816295 | Takahashi H, Maruo Y, Mori A, Iwai M, Sato H, Takeuchi Y: Effect of D256N and Y483D on propofol glucuronidation by human 5'- glucuronosyltransferase (UGT1A9). Basic Clin Pharmacol Toxicol. 2008 Aug;103(2):131-6. For mycophenolic acid, 1-naphthol and the D256N variant lowered glucuronidation activity considerably, compared to Y483D. We investigated the effects of D256N and Y483D, which is located on the common exon of UGT1, on propofol glucuronidation by an in vitro expression study. |
1(0,0,0,1) | Details |
| 7786300 | Gschaidmeier H, Seidel A, Burchell B, Bock KW: Formation of mono- and diglucuronides and other glycosides of benzo (a) pyrene-3,6- by V79 cell-expressed human UDP-glucuronosyltransferases of the UGT1 gene complex. Biochem Pharmacol. 1995 May 26;49(11):1601-6. Therefore, mono- and diglucuronide formation of benzo (a) pyrene-3,6- was investigated and compared to that of structurally related 3,6-dihydroxychrysene and simple phenols (1-naphthol and 4-methylumbelliferone) using V79 cell-expressed human UGT1.6 (= P1) and human UGT1.7 (= P4). |
1(0,0,0,1) | Details |
| 8333863 | Jin CJ, Miners JO, Lillywhite KJ, Mackenzie PI: cDNA cloning and expression of two new members of the human liver UDP-glucuronosyltransferase 2B subfamily. Biochem Biophys Res Commun. 1993 Jul 15;194(1):496-503. The deduced amino acid sequences of UGTs 2B10 and 2B11 share > 76% sequence similarity with other known human liver UGT2B subfamily isoforms and < 48% sequence similarity with UGT1 family proteins. UGT2B11 expressed in COS-7 cells glucuronidated a number of polyhydroxylated estrogens 4-hydroxyestrone and 2-hydroxyestriol) and xenobiotics (4-methylumbelliferone, 1-naphthol, 2- 4-hydroxybiphenyl and |
1(0,0,0,1) | Details |
| 9990312 | Kobayashi T, Yokota H, Ohgiya S, Iwano H, Yuasa A: UDP-glucuronosyltransferase UGT1A7 induced in rat small intestinal mucosa by oral administration of 2-naphthoflavone. Eur J Biochem. 1998 Dec 15;258(3):948-55. In the rat intestine, UDP-glucuronosyltransferase (UGT) isoforms were highly induced by oral administration of 2-naphthoflavone, as shown by intestinal UGT activity toward 1-naphthol (1-NA). S1 mapping showed that induction of the isoforms of the UGT1 family was more pronounced in the liver than in the small intestine and that UGT1A7 was the major UGT1 isoform in the small intestine of vehicle-treated rats and in that of 2-naphthoflavone-treated rats. |
1(0,0,0,1) | Details |
| 12093618 | Yamashiki N, Yokota H, Sakamoto M, Yuasa A: Presence of UDP-glucuronosyltransferase in bovine alveolar macrophages and bronchial epithelial cells. Toxicology. 2002 Jul 15;176(3):221-7. A high level of activity of UGT, which is one of the phase II drug-metabolizing enzymes, toward 1-naphthol was observed in the microsomes of both cell types. Reverse transcriptase-polymerase chain reaction (RT-PCR) amplified the common cDNA region in UGT1A subfamily isoforms, indicating that UGT1A subfamily isoform was expressed in alveolar macrophages and in bronchial epithelial cells of the lung. |
1(0,0,0,1) | Details |
| 11437353 | Soars MG, Smith DJ, Riley RJ, Burchell B: Cloning and characterization of a canine UDP-glucuronosyltransferase. Arch Biochem Biophys. 2001 Jul 15;391(2):218-24. The enzyme expressed stably in V79 cells predominantly catalyzed the glucuronidation of simple, planar phenols (e.g., for 1-naphthol, K (m) = 41 microM, V (max) = 0.07 nmol/min/mg protein), a class of compounds extensively glucuronidated by human UGT1A6. Based on sequence homology and common catalytic activity, this dog UGT1A protein appears to be the canine orthologue of human UGT1A6. |
1(0,0,0,1) | Details |
| 15502008 | Webb LJ, Miles KK, Auyeung DJ, Kessler FK, Ritter JK: Analysis of substrate specificities and tissue expression of rat UDP-glucuronosyltransferases UGT1A7 and UGT1A8. Drug Metab Dispos. 2005 Jan;33(1):77-82. Epub 2004 Oct 22. The UGT1 complex codes for a subfamily of homologous "1A7-like" UDP-glucuronosyltransferases (UGTs), including UGT1A7 and UGT1A8. Other effective UGT1A8 substrates (> 0.1 nmol/mg/min) included 9-OH-benzo [a] pyrene, 1-naphthol, 4-methylumbelliferone, 7-hydroxycoumarin, chrysin, and |
1(0,0,0,1) | Details |
| 9429234 | Ciotti M, Marrone A, Potter C, Owens IS: Genetic polymorphism in the human UGT1A6 (planar UDP-glucuronosyltransferase: pharmacological implications. Pharmacogenetics. 1997 Dec;7(6):485-95. UGT1A6*2 (181 A+ and 184S+) metabolized 4-tert-butylphenol, 3-ethylphenol/4-ethylphenol, butylated anisole and butylated toluene, with the pH 6.4 preference, at only 27-75% of the rate of the wild-type isozyme whereas 1-naphthol, 3-iodophenol, 7-hydroxycoumarin, and 7--4-methylcoumarin were metabolized at essentially the normal level. Both an A to G transition at nucleotide 541 (T181 A) and an A to C transversion at nucleotide 552 (R184S) occurred in exon 1 of the UGT1A6 (UGT1F) gene at the UGT1 locus. |
1(0,0,0,1) | Details |
| 17301691 | Kurkela M, Patana AS, Mackenzie PI, Court MH, Tate CG, Hirvonen J, Goldman A, Finel M: Interactions with other human UDP-glucuronosyltransferases attenuate the consequences of the Y485D mutation on the activity and substrate affinity of UGT1A6. Pharmacogenet Genomics. 2007 Feb;17(2):115-26. Using 1-naphthol as the aglycone substrate, the Km of 6YD for the cosubstrate UDP- was about 50 times higher than in UGT1A6. Owing to exon sharing in the human UGT1A gene, the equivalent mutation is present in all other UGT1As of the affected individuals. |
1(0,0,0,1) | Details |
| 10190968 | Kobayashi T, Tatano A, Yokota H, Onaga T, Watanabe T, Yuasa A: Small intestinal UDP-glucuronosyltransferase sheUGT1A07: partial purification and cDNA cloning from sheep small intestine. Arch Biochem Biophys. 1999 Apr 15;364(2):143-52. The purified preparation containing a one major band (57 kDa) and one minor band (50 kDa) revealed high activities toward xenobiotics such as 1-naphthol (1-NA), and 4-methylumbelliferone. |
0(0,0,0,0) | Details |
| 18981171 | Mackenzie PI, Rogers A, Treloar J, Jorgensen BR, Miners JO, Meech R: Identification of UDP glycosyltransferase 3A1 as a UDP N-acetylglucosaminyltransferase. J Biol Chem. 2008 Dec 26;283(52):36205-10. Epub 2008 Nov 3. In addition to UGT3A1 has activity toward 17alpha-estradiol, 17beta- and the prototypic substrates of the UGT1 and UGT2 forms, and 1-naphthol. |
32(0,1,1,2) | Details |