| Name | sulfotransferase |
|---|---|
| Synonyms | SULT; sulfotransferase |
| Name | 1-naphthol |
|---|---|
| CAS | 1-naphthalenol |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 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 |
| 8363642 | Franklin MR: Induction of rat liver drug-metabolizing enzymes by heterocycle-containing mono-, di-, tri- and tetra-arylmethanes. Biochem Pharmacol. 1993 Aug 17;46(4):683-9. UDP-glucuronosyltransferase (1-naphthol) activity was coinduced by these two compounds. |
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 |
| 10670822 | Bostrom M, Becedas L, DePierre JW: Conjugation of 1-naphthol in primary cell cultures of rat ovarian cells. Chem Biol Interact. 2000 Jan 15;124(2):103-18. The present findings demonstrate that P-UGT is by far the major enzyme conjugating 1-naphthol in the rat ovary and that commonly used inhibitors of P-SULT and CYPs also inhibit P-UGT activity, either directly or via other mechanisms. |
112(1,2,2,2) | Details |
| 3079828 | Hjelle JT, Hazelton GA, Klaassen CD, Hjelle JJ: Glucuronidation and sulfation in rabbit kidney. . J Pharmacol Exp Ther. 1986 Jan;236(1):150-6. UDP-Glucuronosyltransferase and sulfotransferase activities directed toward 1-naphthol were highest in proximal tubules (2.86 +/- 0.13 nmol and 133 +/- 13.1 pmol product formed/min/mg protein, respectively) compared to outer stripe (45% and 64% of proximal tubule activity, respectively) and cortex (61% and 45%, respectively). |
33(0,1,1,3) | Details |
| 1582375 | Jones AL, Hume R, Bamforth KJ, Coughtrie MW: and phenol sulfotransferase activities in human fetal lung. . Early Hum Dev. 1992 Jan;28(1):65-77. Investigation of the thermostability and inhibition by 2,6-dichloro- (DCNP) of the 1-naphthol and sulfotransferase (ST) activities revealed that the ST activity was more thermolabile and more readily inhibited by DCNP than was the 1-naphthol ST activity. |
32(0,1,1,2) | Details |
| 15100179 | Sheng JJ, Saxena A, Duffel MW: Influence of phenylalanines 77 and 138 on the stereospecificity of aryl sulfotransferase IV. Drug Metab Dispos. 2004 May;32(5):559-65. Kinetic studies on the sulfation of the enantiomers of 1,2,3,4-tetrahydro-1-naphthol indicated that the stereospecificity of the sulfotransferase was altered by the substitutions of for either Phe77 or Phe138, but stereospecificity was maintained by substitution at Tyr236. |
32(0,1,1,2) | Details |
| 14508638 | Birkner S, Weber S, Dohle A, Schmahl G, Bolt HM, Follmann W: Activities of drug metabolizing enzymes in bovine colon epithelial cell cultures. Arch Toxicol. 2003 Nov;77(11):621-9. Epub 2003 Sep 24. Whereas activity of amino sulfotransferase (substrate 2-naphthylamine) decreased continuously during the entire culture period, the activity of phenol sulfotransferase (substrate 1-naphthol) decreased only slowly. |
31(0,1,1,1) | Details |
| 2067545 | McMillan JM, Shaddock JG, Casciano DA, Arlotto MP, Leakey JE: Differential stability of drug-metabolizing enzyme activities in primary rat hepatocytes, cultured in the absence or presence of dexamethasone. Mutat Res. 1991 Jul;249(1):81-92. DEX treatment also significantly accelerated the decreases in glutathione-S-transferase activities and in sulfotransferase activities towards 1-naphthol and |
7(0,0,1,2) | Details |
| 12419836 | Teubner W, Meinl W, Glatt H: Stable expression of rat sulfotransferase 1B1 in V79 cells: activation of benzylic to mutagens. Carcinogenesis. 2002 Nov;23(11):1877-84. Sulfotransferase activity towards 1-naphthol was 1020 +/- 220 pmol/min/mg cytosolic protein in V79-rSULT1B1-A cells and 57 +/- 9 pmol/ min/mg in V79-rSULT1B1-B cells. |
7(0,0,1,2) | Details |
| 16806523 | Martin-Skilton R, Coughtrie MW, Porte C: Sulfotransferase activities towards xenobiotics and in two marine fish species (Mullus barbatus and Lepidorhombus boscii): characterization and inhibition by endocrine disrupters. Aquat Toxicol. 2006 Aug 12;79(1):24-30. Epub 2006 May 10. Among the tested compounds, 1-naphthol was the most effective substrate for sulfation, with Vmax/Km ratios several hundred-fold higher than the other substrates examined. |
3(0,0,0,3) | Details |
| 9463486 | Wang J, Falany JL, Falany CN: Expression and characterization of a novel thyroid hormone-sulfating form of cytosolic sulfotransferase from human liver. Mol Pharmacol. 1998 Feb;53(2):274-82. Expressed hST1B2 sulfates small phenols such as 1-naphthol and and thyroid hormones, including 3,3'- reverse and |
3(0,0,0,3) | Details |
| 1863522 | Rao SI, Duffel MW: Benzylic as stereospecific substrates and inhibitors for aryl sulfotransferase. Chirality. 1991;3(2):104-11. Since the benzylic carbon bearing the group can be asymmetric, the possibility of stereochemical control of substrate specificity of the sulfotransferase was investigated with benzylic In the case of 1,2,3,4-tetrahydro-1-naphthol, only the (-)-(R)-enantiomer was a substrate for the enzyme. |
2(0,0,0,2) | Details |
| 18928301 | Tyapochkin E, Cook PF, Chen G: Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase. Biochemistry. 2008 Nov 11;47(45):11894-9. Epub 2008 Oct 18. The SULT1A1-catalyzed reaction was brought to equilibrium by varying substrate (1-naphthol) and initial concentrations. |
2(0,0,0,2) | Details |
| 1397064 | Bamforth KJ, Dalgliesh K, Coughtrie MW: Inhibition of human liver steroid sulfotransferase activities by drugs: a novel mechanism of drug toxicity?. Eur J Pharmacol. 1992 May 1;228(1):15-21. and sulfotransferase activities were strongly inhibited by a number of compounds, with IC50 values ranging between 440 pM and 147 microM. The xenobiotic substrate 1-naphthol was refractory to substantial inhibition, with the exception of clomiphene. |
2(0,0,0,2) | Details |
| 2243343 | Galinsky RE, Johnson DH, Kane RE, Franklin MR: Effect of aging on hepatic biotransformation in female Fischer 344 rats: changes in sulfotransferase activities are consistent with known gender-related changes in pituitary growth hormone secretion in aging animals. J Pharmacol Exp Ther. 1990 Nov;255(2):577-83. UDP glucuronosyltransferase activity toward 1-naphthol, morphine and was unaffected by advanced age, whereas there was a significant correlation between increased age and increased UDP glucuronosyltransferase activity toward |
2(0,0,0,2) | Details |
| 7749597 | Watkins JB 3rd, LaFollette JW, Sanders RA: Biotransformation in Egyptian spiny mouse Acomys cahirinus. Comp Biochem Physiol C Pharmacol Toxicol Endocrinol. 1995 Jan;110(1):101-7. Sulfotransferase activity was high in kidney and intestine of female spiny mice but undetectable in the same tissues in males. UDP-Glucuronosyltransferase activity toward 1-naphthol in both sexes in the kidney was significantly higher than hepatic and intestinal activity. |
1(0,0,0,1) | Details |
| 19053852 | Saruwatari A, Okamura S, Nakajima Y, Narukawa Y, Takeda T, Tamura H: Pomegranate juice inhibits sulfoconjugation in Caco-2 human colon carcinoma cells. J Med Food. 2008 Dec;11(4):623-8. These results indicate that the inhibition of sulfotransferase activity by in Caco-2 cells is responsible for the reductions seen in 1-naphthyl accumulation. Among several fruit juices tested (apple, peach, orange, pineapple, grapefruit, and pomegranate), pomegranate juice potently inhibited the sulfoconjugation of 1-naphthol in Caco-2 cells. |
1(0,0,0,1) | Details |
| 8869819 | Liu L, Klaassen CD: Regulation of hepatic sulfotransferases by steroidal chemicals in rats. Drug Metab Dispos. 1996 Aug;24(8):854-8. -16 alpha-carbonitrile (PCN) has previously been shown to increase sulfotransferase (ST) activity in rats. PCN (75 mg/kg daily for 4 days) increased liver ST activity toward 1-naphthol and and hydroxysteroid ST activities toward and bile acids; but, PCN had no effects on ST activities toward and N--2-acetylaminofluorene (N-OH-2AAF). |
1(0,0,0,1) | Details |
| 2714162 | Kane RE, Lamott J, Franklin MR, Galinsky RE: Perinatal cimetidine exposure has no apparent effect on hepatic drug oxidative or conjugative activity in adult male rat offspring. Dev Pharmacol Ther. 1989;12(2):96-105. Early cimetidine exposure did not alter hepatic oxidative (cytochrome P-450 content or monooxygenase activity) or conjugative (UDP-glucuronosyltransferase activity towards morphine, 1-naphthol, or sulfotransferase activity towards or glycolithocholate) capacities in mature males. Two sulfotransferase isoenzyme activities sulfotransferase 2 and bile salt sulfotransferase I) previously shown to be regulated by gonadal hormones were also unchanged. |
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 |
| 1905411 | Yang CM, Carlson GP: Glucuronidation and sulfation in subcellular fractions and in the isolated perfused rabbit lung: influence of Pharmacology. 1991;42(1):28-35. Glucuronidation and sulfation of 1-naphthol, 7-hydroxycoumarin, 4-nitrocatechol and phenolphthalein were studied in rabbit lung and liver. Pulmonary UDP-glucuronyltransferase and sulfotransferase activities in subcellular fractions were approximately 20-50% of those determined in the liver. |
1(0,0,0,1) | Details |
| 18725199 | Takahashi S, Sakakibara Y, Mishiro E, Kouriki H, Nobe R, Kurogi K, Yasuda S, Liu MC, Suiko M: Molecular cloning, expression, and characterization of mouse amine N-sulfotransferases. Biochem Biophys Res Commun. 2008 Oct 31;375(4):531-5. Epub 2008 Aug 24. By searching the GenBank database, we recently identified a novel mouse cytosolic sulfotransferase (SULT) cDNA (IMAGE Clone ID 679629) and a novel mouse SULT gene (LOC 215895). Kinetic constants of the sulfation of 1-naphthylamine and 1-naphthol by these two enzymes were determined. |
1(0,0,0,1) | Details |
| 9321525 | Oddy EA, Manchee GR, Freeman NM, Ward MA, Coughtrie MW: Purification and characterization of a canine liver phenol sulfotransferase. Drug Metab Dispos. 1997 Oct;25(10):1205-10. Sulfation is an important pathway for metabolism of xenobiotics and potent endogenous compounds and is catalyzed by members of the sulfotransferase enzyme family. We have purified a phenol sulfotransferase from male dog liver cytosol which sulfates simple phenolic compounds such as 1-naphthol and |
1(0,0,0,1) | Details |
| 6959650 | Borchardt RT, Schasteen CS: Phenol sulfotransferase. Biochim Biophys Acta. 1982 Nov 19;708(3):272-9. A phenol sulfotransferase (3-phosphoadenylylsulfate:phenol sulfotransferase, EC 2.8.2.1) has been purified from rat liver using an affinity chromatography system consisting of a -agarose conjugate. The enzyme readily sulfates 2-naphthol, 1-naphthol, and salicylamide, as well as naturally occurring catecholamines. |
1(0,0,0,1) | Details |
| 7874051 | Kim DH, Kim B, Kim HS, Sohng IS, Kobashi K: Sulfation of parabens and tyrosylpeptides by bacterial arylsulfate sulfotransferases. Biol Pharm Bull. 1994 Oct;17(10):1326-8. Arylsulfate sulfotransferase purified from Eubacterium A-44 has higher specific activity than the enzymes from Klebsiella K-36 and Haemophilus |
1(0,0,0,1) | Details |
| 12524029 | Sivapathasundaram S, Sauer MJ, Ioannides C: Xenobiotic conjugation systems in deer compared with cattle and rat. Comp Biochem Physiol C Toxicol Pharmacol. 2003 Jan;134(1):169-73. Cytosolic sulfotransferase activity, monitored using 2-naphthol as substrate, was higher in cattle compared with the rat. |
1(0,0,0,1) | Details |
| 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 |
| 8654197 | Sastry SG, Sanders RA, Veltman JC, Watkins JB 3rd: Minimal effects of two aldose reductase inhibitors, AL-1576 and AL-4114, after subacute topical-ocular dosing on xenobiotic biotransformation in rabbits. Drug Metab Dispos. 1995 Oct;23(10):1094-8. Activities of 1-chloro-2,4-dinitrobenzene glutathione S-transferase, 2-naphthol sulfotransferase, and 1-naphthol UDP-glucuronosyltransferase were not significantly induced in the eight tissues. |
0(0,0,0,0) | 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. |
0(0,0,0,0) | 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. |
0(0,0,0,0) | Details |