| Name | transferase |
|---|---|
| Synonyms | 4' phosphopantetheinyl transferase; 4' phosphopantetheinyl transferase; AASD PPT; AASDHPPT; AASDPPT; Alpha aminoadipic semialdehyde dehydrogenase phosphopantetheinyl transferase; Aminoadipate semialdehyde dehydrogenase phosphopantetheinyl transferase; CGI 80… |
| Name | 1-naphthol |
|---|---|
| CAS | 1-naphthalenol |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 2125759 | Manning BW, Franklin MR: Induction of rat UDP-glucuronosyltransferase and glutathione S-transferase activities by L-buthionine-S,R-sulfoximine without induction of cytochrome P-450. Toxicology. 1990 Dec 17;65(1-2):149-59. Exposure to 30 mM BSO in drinking water for 7 days induced hepatic microsomal UDP-glucuronosyltransferase activity (detergent-activated) toward (250%), 1-naphthol (210%), morphine (130%) and (140%), but not |
0(0,0,0,0) | Details |
| 2105094 | Fong AT, Swanson HI, Dashwood RH, Williams DE, Hendricks JD, Bailey GS: Mechanisms of anti-carcinogenesis by Biochem Pharmacol. 1990 Jan 1;39(1):19-26. Dietary I3C had no significant effect on liver microsomal -glucuronyl-transferase activity, measured using the substrates 1-naphthol and or on cytosolic glutathione S-transferase activity, measured using the substrate styrene oxide. |
0(0,0,0,0) | Details |
| 17178690 | Wolf DC, Allen JW, George MH, Hester SD, Sun G, Moore T, Thai SF, Delker D, Winkfield E, Leavitt S, Nelson G, Roop BC, Jones C, Thibodeaux J, Nesnow S: Toxicity profiles in rats treated with tumorigenic and nontumorigenic triazole conazole fungicides: Propiconazole, triadimefon, and myclobutanil. Toxicol Pathol. 2006;34(7):895-902. diphopho-glucuronosyl transferase (UDPGT), the T4 metabolizing enzyme measured as glucuronidation of 1-naphthol, was induced to the same extent after 30 and 90 days for all three conazoles. |
81(1,1,1,1) | Details |
| 3240719 | Jagadeesan V, Oesch F: Effects of dietary zinc deficiency on the activity of enzymes associated with phase I and II of drug metabolism in Fischer-344 rats: activities of drug metabolising enzymes in zinc deficiency. Drug Nutr Interact. 1988;5(4):403-13. It was observed that the activities of microsomal epoxide hydrolase (with benz (a) pyrene 4-5 oxide as substrate), diphospho glucuronyl transferase (with 1-naphthol as substrate) and cytosolic glutathione-S-transferase (with chlorodinitrobenzene as substrate) were altered exclusively due to zinc deficiency. |
81(1,1,1,1) | Details |
| 3090569 | Pacifici GM, Giuliani L, Calcaprina R: Glucuronidation of 1-naphthol in nuclear and microsomal fractions of the human intestine. Pharmacology. 1986;33(2):103-9. The glucuronyl transferase activity was measured with 1-naphthol as a substrate in nuclear and microsomal fractions of the human intestinal mucosa. |
33(0,1,1,3) | Details |
| 7599146 | Zihnioglu F, Telefoncu A: Diffusion characteristics of -entrapped microsomal -glucuronyl transferase gel beads. Biochim Biophys Acta. 1995 Jun 9;1244(2-3):291-4. Rabbit hepatic microsomal -glucuronyl transferase (EC 2.4.1.17) was immobilized by entrapment in which is an ionotropic gelation agent and the resulting preparation was used as a biocatalyst for the glucuronidation of 1-naphthol in order to study the drug metabolism in vitro and obtaining artificial liver support (detoxification). |
33(0,1,1,3) | Details |
| 7581838 | Zihnioglu F, Telefoncu A: Substrate specificity and the use of -entrapped rabbit hepatic microsomal -glucuronyl transferase for detoxification. Artif Cells Blood Substit Immobil Biotechnol. 1995;23(4):533-43. Rabbit hepatic microsomal -Glucuronyl transferase (EC.2.4.1.17) was immobilized in which is an ionotropic gelatation agent, and the resulting preparation was used as a biocatalyst for the glucuronidation of toxic substances and drugs such as; 1-naphthol, testesterone, and chlorpromazine. |
32(0,1,1,2) | Details |
| 3116724 | Rozman K, Gorski JR, Dutton D, Parkinson A: Effects of and/or thyroidectomy on liver microsomal enzymes and their induction in 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated rats. Toxicology. 1987 Oct 12;46(1):107-17. excess markedly suppressed the activity of liver microsomal UDP-glucuronosyl transferase toward 1-naphthol. |
32(0,1,1,2) | Details |
| 1907143 | Niemann C, Gauthier JC, Richert L, Ivanov MA, Melcion C, Cordier A: Rat adult hepatocytes in primary pure and mixed monolayer culture. Biochem Pharmacol. 1991 Jul 5;42(2):373-9. UPD-glucuronosyl transferase (UDP-GT) activity was measured using 1-naphthol and morphine as substrates. |
31(0,1,1,1) | Details |
| 7839362 | Diener B, Abdel-Latif H, Arand M, Oesch F: Xenobiotic metabolizing enzyme activities and viability are well preserved in EDTA-isolated rat liver parenchymal cells after cryopreservation. Toxicol Appl Pharmacol. 1995 Jan;130(1):149-53. The following phase II enzyme activities were also well maintained after cryopreservation: Phenol sulfotransferase (92%), 1-naphthol UDP-glucuronosyl transferase (95%), soluble epoxide hydrolase (87%), and glutathione S-transferase (88%), determined with broad spectrum substrate 1-chloro-2,4-dinitrobenzene. |
31(0,1,1,1) | Details |
| 14738905 | Nebbia C, Dacasto M, Carletti M: Postnatal development of hepatic oxidative, hydrolytic and conjugative drug-metabolizing enzymes in female horses. Life Sci. 2004 Feb 13;74(13):1605-19. Also the carboxylesterases and uridindiphosphoglucuronyl-transferase (UGT) activity toward 1-naphthol displayed a similar trend, glutathione S-transferase accepting 3,4-dichloronitrobenzene as a substrate being the only enzyme activity showing an age-related decline. |
31(0,1,1,1) | Details |
| 7157840 | Pacifici GM, Davies DS, Whyte C, Boobis AR: Tissue differences in the ontogeny of inducibility of drug-metabolizing enzymes by 3-methylcholanthrene in the rabbit. Xenobiotica. 1982 Sep;12(9):591-8. The effects of treatment of rabbits of different ages with 3-methylcholanthrene on cytochrome P-450 content, and benzo [a] pyrene hydroxylase, epoxide hydrolase, S-epoxide transferase, 1-naphthol glucuronyl transferase and morphine glucuronyl transferase activities of liver, kidney and lung have been investigated. 2. |
13(0,0,2,3) | Details |
| 2509439 | Yokota H, Ohgiya N, Ishihara G, Ohta K, Yuasa A: Purification and properties of UDP-glucuronyltransferase from kidney microsomes of beta-naphthoflavone-treated rat. J Biochem. 1989 Aug;106(2):248-52. These procedures gave about 39-fold purification and 11.5% yield of the transferase activity toward 1-naphthol. |
7(0,0,1,2) | Details |
| 1521595 | Galinsky RE, Manning BW, Kimura RE, Franklin MR: Changes in conjugative enzyme activity and metabolism in young and senescent male F-344 rats following prolonged exposure to buthionine sulfoximine. Exp Gerontol. 1992;27(2):221-32. BSO treatment increased the partial clearance to by 90% and 41% in young and old rats, respectively, and similarly, induced and 1-naphthol UDP-glucuronosyl transferase activities to a greater extent in young versus senescent animals. |
7(0,0,1,2) | Details |
| 9193647 | Davis T, Sabir JS, Tavassoli M, Shall S: Purification, characterisation, and molecular cloning of a chicken erythroblast mono (ADP-ribosyl) transferase. Adv Exp Med Biol. 1997;419:145-54. Among the more effective inhibitors are 1,4 naphthoquinone, 5,8-dihydroxy-1,4-naphthoquinone, 4-amino-1-naphthol and 1,2-naphthoquinone. |
7(0,0,0,7) | Details |
| 1494890 | Utesch D, Arand M, Thomas H, Petzinger E, Oesch F: Xenobiotic-metabolizing enzyme activities in hybrid cell lines established by fusion of primary rat liver parenchymal cells with hepatoma cells. Xenobiotica. 1992 Dec;22(12):1451-7. These enzyme activities were significantly higher in HPCT and correspond to about 1-10% the activities measured in PC. 4. 1-Naphthol UPD-glucuronosyl transferase activity was about 20% in FAO and about 100% in HPCT compared to PC. 5. |
6(0,0,1,1) | Details |
| 6781487 | Weatherill PJ, Kennedy SM, Burchell B: Immunochemical comparison of UDP-glucuronyltransferase from Gunn- and Wistar-rat livers. Biochem J. 1980 Oct 1;191(1):155-63. Immunoglobulin G purified from this antiserum immunoprecipitated transferase activities towards and 1-naphthol. 7. |
6(0,0,1,1) | Details |
| 6439213 | Morrison MH, Hawksworth GM: conjugation by hepatic microsomal fractions isolated from streptozotocin-induced diabetic rats. Biochem Pharmacol. 1984 Dec 1;33(23):3833-8. The hepatic glucuronidation of 1-naphthol and (3-methylcholanthrene inducible substrates of glucuronyltransferase, GT 1) was found to be deficient in freshly prepared untreated "native" microsomes from streptozotocin-induced diabetic male rats. This sex difference in the glucuronidation of the GT 1 substrates was abolished by detergent activation of the transferase enzyme in vitro. |
3(0,0,0,3) | Details |
| 7581839 | Zihnioglu F, Telefoncu A: Preparation and characterization of -entrapped microsomal -glucuronyl transferase. Artif Cells Blood Substit Immobil Biotechnol. 1995;23(4):545-52. Chemical and physical characterization were made by using 1-naphthol as substrate. |
2(0,0,0,2) | Details |
| 3149280 | Yokota H, Yuasa A, Sato R: Purification and properties of a form of UDP-glucuronyltransferase from liver microsomes of 3-methylcholanthrene-treated rats. J Biochem. 1988 Oct;104(4):531-6. It catalyzed the glucuronidation of not only phenolic xenobiotics such as 1-naphthol, and but also which is an endogenous compound. After removal of the detergent (Emulgen 911), the transferase activity was stimulated by various phospholipids, about 10-fold activation being attained with and lysophosphatidylcholine. |
2(0,0,0,2) | Details |
| 8147909 | Yokota H, Ikezoe H, Inaba T, Sanda D, Yuasa A, Kasai N: Increase of UDP-glucuronosyltransferase activities toward xenobiotics during the development of hereditary hepatitis in LEC rats. Biochem Pharmacol. 1994 Mar 15;47(6):1091-3. After 8 weeks of age, the transferase activities of LEA rats towards all substrates tested, except for decreased slightly during the next 24 weeks. In LEC rats, the transferase activities towards and several phenolic xenobiotics, such as 1-naphthol and 4-methylumbelliferone, but not 4-hydroxybiphenyl, increased about 2-fold at 16 weeks of age. |
2(0,0,0,2) | Details |
| 6811722 | Adachi S, Fujita S, Uesugi T: Effect of 1-m-tolueneazo-2-naphthol on hepatic drug metabolism. J Pharmacobiodyn. 1982 Apr;5(4):273-7. Effect of potent cytochrome P-448 inducer, 1-m-tolueneazo-2-naphthol (m-TAN) on hepatic microsomal UDP-glucuronyl-transferase (UDPGT) activity was studied. The UDPGT activities towards 1-naphthol and chloramphenicol were increased up to 6,2.5 and 1.8 folds of control levels respectively, in microsomes from m-TAN treated rats. 3-Methylcholanthrene, on the other hand, caused 4 and 2 fold increase in UDPGT activities towards and 1-naphthol, respectively, but did not cause significant increase in UDPGT activity towards chloramphenicol. |
1(0,0,0,1) | Details |
| 3140501 | Pacifici GM, Franchi M, Bencini C, Repetti F, Di Lascio N, Muraro GB: Tissue distribution of drug-metabolizing enzymes in humans. Xenobiotica. 1988 Jul;18(7):849-56. The activities of the ethoxycoumarin O-deethylase (ECOD), epoxide hydrolase (EH), UDP-glucuronyl transferase (GT), glutathione S-transferase (GST), acetyl transferase (AT) and sulphotransferase (ST) were measured in 6 liver, 8 lung, 8 kidney, 8 intestinal mucosa and 22 urinary bladder mucosa specimens from human subjects. EH and GT were studied with styrene oxide and 1-naphthol, respectively, as substrates, GST, AT and ST were studied with benzo (a) pyrene-4,5-oxide, and 2-naphthol, respectively. 2. |
1(0,0,0,1) | Details |
| 1292927 | Vajro P, Thaler MM, Blanckaert N: Failure of expression of the phenobarbital-induced enhancement of UDP-glycosyltransferases in native, sealed endoplasmic reticulum vesicles from rat liver. Enzyme. 1992;46(4-5):169-78. We examined the effect of phenobarbital on UDP-glucosyltransferase and the UDP-glucuronyltransferase activities towards and 1-naphthol using native rat liver microsomes with verified vesicle integrity. In contrast, none of the transferase activities tested were significantly enhanced by phenobarbital treatment when the enzymic activities were assayed in sealed microsomes. |
1(0,0,0,1) | Details |
| 6416300 | Koster AS, Noordhoek J: Kinetic properties of the rat intestinal microsomal 1-naphthol:UDP-glucuronosyl transferase. Biochim Biophys Acta. 1983 Nov 22;761(1):76-85. The enzyme appeared to follow an ordered sequential bireactant mechanism in which 1-naphthol and UDP- (UDPGlcUA) are the first and second binding substrates and UDP and 1-naphthol the first and second products, respectively. |
1(0,0,0,1) | Details |
| 16819192 | Naganuma M, Saruwatari A, Okamura S, Tamura H: and modulate the conjugation of 1-naphthol in Caco-2 cells. Biol Pharm Bull. 2006 Jul;29(7):1476-9. In addition, was found to strongly inhibit in vitro phenol sulfotransferase (SULT) activity and demonstrate moderate inhibitory properties against UDP-glucuronosyl transferase (UGT) activity in Caco-2 cells (IC (50)=0.17 mg/ml and 0.62 mg/ml, respectively). |
1(0,0,0,1) | Details |
| 101211 | Wishart GJ: Functional heterogeneity of UDP-glucuronosyltransferase as indicated by its differential development and inducibility by glucocorticoids. Biochem J. 1978 Aug 15;174(2):485-9. The relationship of these two groups of transferase activities to other similar groups observed during induction by xenobiotics and enzyme purification is discussed. Between days 16 and 20 of gestation, enzyme activities towards the substrates 2- 1-naphthol, 4-methylumbelliferone and (the 'late foetal' group) surge to reach adult values, while activities towards beta- morphine, phenolphthalein, and chloramphenicol (the 'neonatal' group) remain negligible or at less than 10% of adult values. 3. |
1(0,0,0,1) | Details |
| 1386480 | Goon D, Klaassen CD: Effects of microsomal enzyme inducers upon UDP- concentration and UDP-glucuronosyltransferase activity in the rat intestine and liver. Toxicol Appl Pharmacol. 1992 Aug;115(2):253-60. This study was conducted to evaluate UDP-glucuronosyl-transferase (UDP-GT) activity, UDP- (UDP-GA) concentration, and UDP- concentration in the rat intestine and liver following oral administration of butylated hydroxyanisole (BHA), benzo [a] pyrene (BaP), 3-methylcholanthrene (3MC), phenobarbital (PB), -16 alpha-carbonitrile (PCN), 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), or trans-stilbene oxide (TSO). Microsomal UDP-GT activity was assayed in vitro with (AA), harmol (HA), and 1-naphthol (NA) as the aglycones. |
1(0,0,0,1) | Details |
| 6412703 | Burchell B, Pratt GJ, Duffy I, West L: Identification of increased amounts of UDP-glucuronyltransferase protein in phenobarbital-treated chick-embryo liver cells. Biochem J. 1983 Aug 15;214(2):517-23. UDP-glucuronyltransferase activity of neonatal-chick liver or phenobarbital-treated chick-embryo liver catalysed the glucuronidation of 1-naphthol, and 2- Liver microsomal transferase activity towards the three phenols was increased approx. 20-50-fold by phenobarbital treatment of chick embryos or by transfer of liver cells into tissue culture. |
1(0,0,0,1) | Details |
| 6418879 | Rush GF, Newton JF, Hook JB: Sex differences in the excretion of conjugates: the role of intrarenal glucuronidation. J Pharmacol Exp Ther. 1983 Dec;227(3):658-62. UDP-glucuronyl-transferase activity in renal microsomes prepared from male and female rats toward was 0.21 +/- 0.09 nmol/min/mg of protein and 0.91 +/- 0.02 nmol/min/mg of protein, respectively. Similar in vitro sex differences were also observed with 1-naphthol as the aglycone. |
1(0,0,0,1) | Details |
| 2108023 | Noort D, Coughtrie MW, Burchell B, van der Marel GA, van Boom JH, van der Gen A, Mulder GJ: Inhibition of UDP-glucuronosyltransferase activity by possible transition-state analogues in rat-liver microsomes. Eur J Biochem. 1990 Mar 10;188(2):309-12. In general glucuronidation was more effectively inhibited than that of 1-naphthol, or 2-(1-Naphthyl) ethyl-UDP and 2,2,2-(triphenyl) ethyl-UDP were the most effective inhibitors. The various UDP derivatives showed differences in their abilities to inhibit the glucuronidation of the four acceptor substrates, supporting the concept that the different forms of UDP-glucuronosyl transferase have different active sites. |
1(0,0,0,1) | Details |
| 6431226 | Mackenzie PI, Lang MA, Owens IS: Effect of different detergent systems on the molecular size of UDP glucuronosyltransferase and other microsomal drug-metabolizing enzymes. Membr Biochem. 1984;5(3):193-207. CHAPS alone also generated similarly sized particles under conditions in which UDP glucuronosyltransferase activity toward 1-naphthol and morphine was two to about twenty times greater, respectively, than with the combination of detergents. This finding suggests that the zwitterionic CHAPS is superior to other detergent systems for studies concerned with the purification of transferase enzymes, a microsomal system in which investigation of the number of different forms has been hampered by the instability of the enzyme upon solubilization and subsequent manipulation. |
1(0,0,0,1) | Details |
| 1949033 | Franklin MR: Drug metabolizing enzyme induction by simple diaryl pyridines; 2-substituted isomers selectively increase only conjugation enzyme activities, 4-substituted isomers also induce cytochrome P450. Toxicol Appl Pharmacol. 1991 Oct;111(1):24-32. All five 2-substituted pyridines investigated increased rat hepatic UDP-glucuronosyltransferase activities toward three aglycones (morphine, and 1-naphthol) without inducing cytochrome P450. UDP-glucuronosyl-transferase activity by the 4-substituted pyridines was increased to a much lesser extent than seen for the equivalent 2-isomers. |
1(0,0,0,1) | Details |
| 6803311 | Bansal SK, Li HC, Holmes G, Gessner T: On the functional heterogeneity of -glucuronyl transferase of mouse liver microsomes. Res Commun Chem Pathol Pharmacol. 1982 Feb;35(2):291-302. Of these three peaks, only peak II contained activities towards all the substrates tested: 1-naphthol, morphine, and |
1(0,0,0,1) | Details |
| 1939026 | Yokota H, Fukuda T, Yuasa A: Differential effects of phospholipids on two similar forms of UDP-glucuronyltransferase purified from rat liver and kidney microsomes. J Biochem. 1991 Jul;110(1):50-3. However, the effects of phospholipids on these enzymes were extremely different. 1-Naphthol glucuronizing activity of GT-1 was increased 7.5-8-fold by lysophosphatidylcholine, but the activity of GT-2 was increased only 3-3.6-fold. The transferase activity of GT-1 toward 4-methylumbelliferone was increased 2-2.5-fold by dilauroylphosphatidylcholine, but that of GT-2 was reduced, while its glucuronidation activity was increased 1.5-fold by the phospholipid. |
1(0,0,0,1) | Details |
| 3929791 | Andersson T, Pesonen M, Johansson C: Differential induction of cytochrome P-450-dependent monooxygenase, epoxide hydrolase, glutathione transferase and UDP glucuronosyl transferase activities in the liver of the rainbow trout by beta-naphthoflavone or Clophen A50. Biochem Pharmacol. 1985 Sep 15;34(18):3309-14. Glutathione transferase activity towards 1-chloro 2,4 dinitrobenzene and UDP glucuronosyltransferase activities towards 1-naphthol and were increased 1.4 to 3.0-fold by beta-naphthoflavone or Clophen A50. |
1(0,0,0,1) | Details |
| 1898504 | Arand M, Coughtrie MW, Burchell B, Oesch F, Robertson LW: Selective induction of UDP-glucuronosyl-transferase by perfluorodecanoic acid. Chem Biol Interact. 1991;77(1):97-105. The induced state was stable for at least 3 weeks. (2) Glucuronidation of 1-naphthol, morphine and was decreased to half of the control values. |
1(0,0,0,1) | Details |
| 1676661 | Manning BW, Franklin MR, Galinsky RE: Drug metabolizing enzyme changes after chronic buthionine sulfoximine exposure modify disposition in rats. Drug Metab Dispos. 1991 Mar-Apr;19(2):498-502. BSO treatment increased microsomal UDP-glucuronosyltransferase activity toward three xenobiotic aglycones, 1-naphthol, and morphine by 308, 61, and 66%, respectively (p less than 0.05), but not toward or |
0(0,0,0,0) | Details |
| 15684482 | Okamura S, Suzuki K, Yanase M, Koizumi M, Tamura HO: The effects of coffee on conjugation reactions in human colon carcinoma cells. Biol Pharm Bull. 2005 Feb;28(2):271-4. After supplementing Caco-2 cultures with both 1-naphthol (200 microM) and various concentrations of coffee, the accumulation of 1-naphthyl and in the growth medium was determined by analytical HPLC over a 24-h period. |
0(0,0,0,0) | Details |
| 6412704 | Scragg I, Pollard M, Burchell B, Dutton GJ: The temporary postnatal decline in glucuronidation of certain phenols by rat liver. Biochem J. 1983 Aug 15;214(2):533-7. The profile of this trough and its time of occurrence (maximal over 13-16 days) are almost identical with the two substrates 2- and 1-naphthol, whose rates of glucuronidation differ 10-fold. |
0(0,0,0,0) | Details |