Arylsulfotransferase: A sulfotransferase that catalyzes the sulfation of a phenol in the presence of 3'-phosphoadenylylsulfate as sulfate donor to yield an aryl sulfate and adenosine 3',5'-bisphosphate. A number of aromatic compounds can act as acceptors; however, organic hydroxylamines are not substrates. Sulfate conjugation by this enzyme is a major pathway for the biotransformation of phenolic and catechol drugs as well as neurotransmitters. EC 2.8.2.1.Sulfotransferases: Enzymes which transfer sulfate groups to various acceptor molecules. They are involved in posttranslational sulfation of proteins and sulfate conjugation of exogenous chemicals and bile acids. EC 2.8.2.Receptors, Aryl Hydrocarbon: Cytoplasmic proteins that bind certain aryl hydrocarbons, translocate to the nucleus, and activate transcription of particular DNA segments. AH receptors are identified by their high-affinity binding to several carcinogenic or teratogenic environmental chemicals including polycyclic aromatic hydrocarbons found in cigarette smoke and smog, heterocyclic amines found in cooked foods, and halogenated hydrocarbons including dioxins and polychlorinated biphenyls. No endogenous ligand has been identified, but an unknown natural messenger with a role in cell differentiation and development is suspected.Antigens, CD98 Heavy Chain: A transmembrane glycoprotein subunit that can dimerize with a variety of light chain subunits (ANTIGENS, CD98 LIGHT CHAINS). This protein subunit serves a diverse array of functions including amino acid transport and cell fusion. Its function is altered depending which of the light chain subunits it interacts with.Phosphoadenosine Phosphosulfate: 3'-Phosphoadenosine-5'-phosphosulfate. Key intermediate in the formation by living cells of sulfate esters of phenols, alcohols, steroids, sulfated polysaccharides, and simple esters, such as choline sulfate. It is formed from sulfate ion and ATP in a two-step process. This compound also is an important step in the process of sulfur fixation in plants and microorganisms.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Dehydroepiandrosterone: A major C19 steroid produced by the ADRENAL CORTEX. It is also produced in small quantities in the TESTIS and the OVARY. Dehydroepiandrosterone (DHEA) can be converted to TESTOSTERONE; ANDROSTENEDIONE; ESTRADIOL; and ESTRONE. Most of DHEA is sulfated (DEHYDROEPIANDROSTERONE SULFATE) before secretion.Minoxidil: A potent direct-acting peripheral vasodilator (VASODILATOR AGENTS) that reduces peripheral resistance and produces a fall in BLOOD PRESSURE. (From Martindale, The Extra Pharmacopoeia, 30th ed, p371)Sulfurtransferases: Enzymes which transfer sulfur atoms to various acceptor molecules. EC 2.8.1.Sulfates: Inorganic salts of sulfuric acid.Steryl-Sulfatase: An arylsulfatase with high specificity towards sulfated steroids. Defects in this enzyme are the cause of ICHTHYOSIS, X-LINKED.Carbon-Carbon Double Bond Isomerases: Enzymes that catalyze the shifting of a carbon-carbon double bond from one position to another within the same molecule. EC 5.3.3.3-Hydroxysteroid Dehydrogenases: Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.Hydroxysteroid Dehydrogenases: Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.Amidine-Lyases: These enzymes catalyze the elimination of ammonia from amidines with the formation of a double bond. EC 4.3.2.Steroids: A group of polycyclic compounds closely related biochemically to TERPENES. They include cholesterol, numerous hormones, precursors of certain vitamins, bile acids, alcohols (STEROLS), and certain natural drugs and poisons. Steroids have a common nucleus, a fused, reduced 17-carbon atom ring system, cyclopentanoperhydrophenanthrene. Most steroids also have two methyl groups and an aliphatic side-chain attached to the nucleus. (From Hawley's Condensed Chemical Dictionary, 11th ed)Ketosteroids: Steroid derivatives formed by oxidation of a methyl group on the side chain or a methylene group in the ring skeleton to form a ketone.Bile Acids and Salts: Steroid acids and salts. The primary bile acids are derived from cholesterol in the liver and usually conjugated with glycine or taurine. The secondary bile acids are further modified by bacteria in the intestine. They play an important role in the digestion and absorption of fat. They have also been used pharmacologically, especially in the treatment of gallstones.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Influenzavirus A: A genus in the family ORTHOMYXOVIRIDAE causing influenza and other diseases in humans and animals. It contains many strains as well as antigenic subtypes of the integral membrane proteins hemagglutinin (HEMAGGLUTININS) and NEURAMINIDASE. The type species is INFLUENZA A VIRUS.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Recombinant Proteins: Proteins prepared by recombinant DNA technology.Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Immunoglobulin Fab Fragments: Univalent antigen-binding fragments composed of one entire IMMUNOGLOBULIN LIGHT CHAIN and the amino terminal end of one of the IMMUNOGLOBULIN HEAVY CHAINS from the hinge region, linked to each other by disulfide bonds. Fab contains the IMMUNOGLOBULIN VARIABLE REGIONS, which are part of the antigen-binding site, and the first IMMUNOGLOBULIN CONSTANT REGIONS. This fragment can be obtained by digestion of immunoglobulins with the proteolytic enzyme PAPAIN.Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.Benzofurans: Compounds that contain a BENZENE ring fused to a furan ring.Neuroprotective Agents: Drugs intended to prevent damage to the brain or spinal cord from ischemia, stroke, convulsions, or trauma. Some must be administered before the event, but others may be effective for some time after. They act by a variety of mechanisms, but often directly or indirectly minimize the damage produced by endogenous excitatory amino acids.Biotransformation: The chemical alteration of an exogenous substance by or in a biological system. The alteration may inactivate the compound or it may result in the production of an active metabolite of an inactive parent compound. The alterations may be divided into METABOLIC DETOXICATION, PHASE I and METABOLIC DETOXICATION, PHASE II.Periodicals as Topic: A publication issued at stated, more or less regular, intervals.Arylamine N-Acetyltransferase: An enzyme that catalyzes the transfer of acetyl groups from ACETYL-COA to arylamines. It can also catalyze acetyl transfer between arylamines without COENZYME A and has a wide specificity for aromatic amines, including SEROTONIN. However, arylamine N-acetyltransferase should not be confused with the enzyme ARYLALKYLAMINE N-ACETYLTRANSFERASE which is also referred to as SEROTONIN ACETYLTRANSFERASE.PubMed: A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.BooksPublishing: "The business or profession of the commercial production and issuance of literature" (Webster's 3d). It includes the publisher, publication processes, editing and editors. Production may be by conventional printing methods or by electronic publishing.MEDLINE: The premier bibliographic database of the NATIONAL LIBRARY OF MEDICINE. MEDLINE® (MEDLARS Online) is the primary subset of PUBMED and can be searched on NLM's Web site in PubMed or the NLM Gateway. MEDLINE references are indexed with MEDICAL SUBJECT HEADINGS (MeSH).Serial Publications: Publications in any medium issued in successive parts bearing numerical or chronological designations and intended to be continued indefinitely. (ALA Glossary of Library and Information Science, 1983, p203)Search Engine: Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.Information Storage and Retrieval: Organized activities related to the storage, location, search, and retrieval of information.Barth Syndrome: Rare congenital X-linked disorder of lipid metabolism. Barth syndrome is transmitted in an X-linked recessive pattern. The syndrome is characterized by muscular weakness, growth retardation, DILATED CARDIOMYOPATHY, variable NEUTROPENIA, 3-methylglutaconic aciduria (type II) and decreases in mitochondrial CARDIOLIPIN level. Other biochemical and morphological mitochondrial abnormalities also exist.Leukemia Virus, Bovine: The type species of DELTARETROVIRUS that causes a form of bovine lymphosarcoma (ENZOOTIC BOVINE LEUKOSIS) or persistent lymphocytosis.Tripterygium: A plant genus of the family CELASTRACEAE that is a source of triterpenoids and diterpene epoxides such as triptolide.Medication Adherence: Voluntary cooperation of the patient in taking drugs or medicine as prescribed. This includes timing, dosage, and frequency.Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.Adolescent Psychiatry: The medical science that deals with the origin, diagnosis, prevention, and treatment of mental disorders in individuals 13-18 years.Child Psychiatry: The medical science that deals with the origin, diagnosis, prevention, and treatment of mental disorders in children.Bibliometrics: The use of statistical methods in the analysis of a body of literature to reveal the historical development of subject fields and patterns of authorship, publication, and use. Formerly called statistical bibliography. (from The ALA Glossary of Library and Information Science, 1983)Publications: Copies of a work or document distributed to the public by sale, rental, lease, or lending. (From ALA Glossary of Library and Information Science, 1983, p181)Attention Deficit Disorder with Hyperactivity: A behavior disorder originating in childhood in which the essential features are signs of developmentally inappropriate inattention, impulsivity, and hyperactivity. Although most individuals have symptoms of both inattention and hyperactivity-impulsivity, one or the other pattern may be predominant. The disorder is more frequent in males than females. Onset is in childhood. Symptoms often attenuate during late adolescence although a minority experience the full complement of symptoms into mid-adulthood. (From DSM-V)Academies and Institutes: Organizations representing specialized fields which are accepted as authoritative; may be non-governmental, university or an independent research organization, e.g., National Academy of Sciences, Brookings Institution, etc.Peer Group: Group composed of associates of same species, approximately the same age, and usually of similar rank or social status.Video Games: A form of interactive entertainment in which the player controls electronically generated images that appear on a video display screen. This includes video games played in the home on special machines or home computers, and those played in arcades.Videotape Recording: Recording of visual and sometimes sound signals on magnetic tape.Journal Impact Factor: A quantitative measure of the frequency on average with which articles in a journal have been cited in a given period of time.Peer Review, Research: The evaluation by experts of the quality and pertinence of research or research proposals of other experts in the same field. Peer review is used by editors in deciding which submissions warrant publication, by granting agencies to determine which proposals should be funded, and by academic institutions in tenure decisions.Peer Review: An organized procedure carried out by a select committee of professionals in evaluating the performance of other professionals in meeting the standards of their specialty. Review by peers is used by editors in the evaluation of articles and other papers submitted for publication. Peer review is used also in the evaluation of grant applications. It is applied also in evaluating the quality of health care provided to patients.

Sulfating-activity and stability of cDNA-expressed allozymes of human phenol sulfotransferase, ST1A3*1 ((213)Arg) and ST1A3*2 ((213)His), both of which exist in Japanese as well as Caucasians. (1/185)

We recently found single amino acid substitutions ((213)Arg/His and (223)Met/Val) in polymorphic human phenol-sulfating phenol sulfotransferase (SULT: cDNAs encoding ST1A3, P PST or HAST1/2) among Caucasians and African-Americans. In a Japanese population (n = 143), allele frequencies of (213)Arg and (213)His were 83.2 and 16. 8%, respectively, but the (223)Val allele was not found. (213)His homozygosity was reportedly associated with both very low (>7-fold) sulfating activities of p-nitrophenol (at 4 microM) and low thermostability in platelets. Sulfating-activity determinations using recombinant (213)Arg- and (213)His-forms (ST1A3*1 and ST1A3*2, respectively) did not, however, reveal appreciable deficiency in [(35)S]3'-phosphoadenosine 5'-phosphosulfate (PAPS)-dependent sulfation of p-nitrophenol (4 microM) by ST1A3*2 (7.5 vs. 10.2 nmol/min/nmol SULT for ST1A3). Kinetic parameters for p-nitrophenol for p-nitrophenol sulfation supported the slight decrease in sulfating activities at 4 microM (K(m), 0.82 vs. 1.75 microM; V(max), 13.2 vs. 13.1 nmol/min/nmol SULT, respectively, for ST1A3*1 and *2). p-Nitrophenyl sulfate-dependent 2-naphthol sulfation by ST1A3*2 was 69% of that by ST1A3*1 (p<0.05). However, ST1A3*2 was remarkably unstable at 45 and 37 degrees C as compared to ST1A3*1. The lower p-nitrophenol sulfating activity of ST1A3*2 may explain the lower platelet p-nitrophenol sulfation in ST1A3*2 homozygotes. Protein instability and ST1A3 gene regulation may be both involved in the polymorphism of p-nitrophenol sulfation in human tissues.  (+info)

Photoaffinity labeling probe for the substrate binding site of human phenol sulfotransferase (SULT1A1): 7-azido-4-methylcoumarin. (2/185)

A novel fluorescent photoactive probe 7-azido-4-methylcoumarin (AzMC) has been characterized for use in photoaffinity labeling of the substrate binding site of human phenol sulfotransferase (SULT1A1 or P-PST-1). For the photoaffinity labeling experiments, SULT1A1 cDNA was expressed in Escherichia coli as a fusion protein to maltose binding protein (MBP) and purified to apparent homogeneity over an amylose column. The maltose moiety was removed by Factor Xa cleavage. Both MBSULT1A1 and SULT1A1 were efficiently photolabeled with AzMC. This labeling was concentration dependent. In the absence of light, AzMC competitively inhibited the sulfation of 4MU catalyzed by SULT1A1 (Ki = 0.47 +/- 0.05 mM). Moreover, enzyme activity toward 2-naphthol was inactivated in a time- and concentration-dependent manner. SULT1A1 inactivation by AzMC was protected by substrate but was not protected by cosubstrate. These results indicate that photoaffinity labeling with AzMC is highly suitable for the identification of the substrate binding site of SULT1A1. Further studies are aimed at identifying which amino acids modified by AzMC are localized in the binding site.  (+info)

X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity. (3/185)

Humans are one of the few species that produce large amounts of catecholamine sulfates, and they have evolved a specific sulfotransferase, SULT1A3 (M-PST), to catalyze the formation of these conjugates. An orthologous protein has yet to be found in other species. To further our understanding of the molecular basis for the unique substrate selectivity of this enzyme, we have solved the crystal structure of human SULT1A3, complexed with 3'-phosphoadenosine 5'-phosphate (PAP), at 2.5 A resolution and carried out quantitative structure-activity relationship (QSAR) analysis with a series of phenols and catechols. SULT1A3 adopts a similar fold to mouse estrogen sulfotransferase, with a central five-stranded beta-sheet surrounded by alpha-helices. SULT1A3 is a dimer in solution but crystallized with a monomer in the asymmetric unit of the cell, although dimer interfaces were formed by interaction across crystallographic 2-fold axes. QSAR analysis revealed that the enzyme is highly selective for catechols, and catecholamines in particular, and that hydrogen bonding groups and lipophilicity (cLogD) strongly influenced K(m). We also investigated further the role of Glu(146) in SULT1A3 using site-directed mutagenesis and showed that it plays a key role not only in defining selectivity for dopamine but also in preventing many phenolic xenobiotics from binding to the enzyme.  (+info)

Sulfation of "estrogenic" alkylphenols and 17beta-estradiol by human platelet phenol sulfotransferases. (4/185)

We have investigated the ability of alkylphenols to act as substrates and/or inhibitors of phenol sulfotransferase enzymes in human platelet cytosolic fractions. Our results indicate: (i) straight chain alkylphenols do not interact with the monoamine-sulfating phenol sulfotransferase (SULT1A3); (ii) short chain 4-n-alkylphenols (C < 8) are substrates for the phenol-sulfating enzymes (SULT1A1/2), which exhibit two activity maxima against substrates with alkyl chain lengths of C1-2 and C4-5; (iii) long chain 4-n-substituted alkylphenols (C >/= 8) are poor substrates and act as inhibitors of SULT1A1/2; (iv) human platelets contain two activities, of low and high affinity, capable of sulfating 17beta-estradiol, and 4-n-nonylphenol is a partial mixed inhibitor of the low affinity form of this activity. We conclude that by acting either as substrates or inhibitors of SULT1A1/2, alkylphenols may influence the sulfation, and hence the excretion, of estrogens and other phenol sulfotransferase substrates in humans.  (+info)

Human phenol sulfotransferases hP-PST and hM-PST activate propane 2-nitronate to a genotoxicant. (5/185)

The industrial solvent 2-nitropropane (2-NP) is a genotoxic hepatocarcinogen in rats. The genotoxicity of the compound in rats has been attributed to sulfotransferase-mediated formation of DNA-reactive nitrenium ions from the anionic form of 2-NP, propane 2-nitronate (P2N). Whether human sulfotransferases are capable of activating P2N is unknown. In the present study we have addressed this question by investigating the genotoxicity of P2N in various V79-derived cell lines engineered for expression of individual forms of human sulfotransferases, the phenol-sulfating and the monoamine-sulfating phenol sulfotransferases (hP-PST and hM-PST) and the human hydroxysteroid sulfotransferase (hHST). Genotoxicity was assessed by measuring the induction of DNA repair synthesis and by analyzing the formation of DNA modifications. P2N induced repair synthesis in V79-hP-PST and V79-hM-PST cells, whereas induction of repair synthesis in V79-hHST cells was negligible. P2N also resulted in the formation of 8-aminodeoxyguanosine and increased the level of 8-oxodeoxyguanosine in V79-hP-PST cells, but not in the parental V79-MZ cells, which do not show any sulfotransferase activity. Acetone oxime, the tautomeric form of the first reduction product of 2-NP, 2-nitrosopropane, was inactive in all cell lines. The results show that the human phenol sulfotransferases P-PST and M-PST are capable of metabolically activating P2N (P-PST >> M-PST) and that the underlying mechanism is apparently identical to that resulting in the activation of P2N in rat liver, where 2-NP causes carcinomas. These results support the notion that 2-NP should be regarded as a potential human carcinogen.  (+info)

The ssu locus plays a key role in organosulfur metabolism in Pseudomonas putida S-313. (6/185)

Pseudomonas putida S-313 can utilize a broad range of aromatic sulfonates as sulfur sources for growth in sulfate-free minimal medium. The sulfonates are cleaved monooxygenolytically to yield the corresponding phenols. miniTn5 mutants of strain S-313 which were no longer able to desulfurize arylsulfonates were isolated and were found to carry transposon insertions in the ssuEADCBF operon, which contained genes for an ATP-binding cassette-type transporter (ssuABC), a two-component reduced flavin mononucleotide-dependent monooxygenase (ssuED) closely related to the Escherichia coli alkanesulfonatase, and a protein related to clostridial molybdopterin-binding proteins (ssuF). These mutants were also deficient in growth with a variety of other organosulfur sources, including aromatic and aliphatic sulfate esters, methionine, and aliphatic sulfonates other than the natural sulfonates taurine and cysteate. This pleiotropic phenotype was complemented by the ssu operon, confirming its key role in organosulfur metabolism in this species. Further complementation analysis revealed that the ssuF gene product was required for growth with all of the tested substrates except methionine and that the oxygenase encoded by ssuD was required for growth with sulfonates or methionine. The flavin reductase SsuE was not required for growth with aliphatic sulfonates or methionine but was needed for growth with arylsulfonates, suggesting that an alternative isozyme exists for the former compounds that is not active in transformation of the latter substrates. Aryl sulfate ester utilization was catalyzed by an arylsulfotransferase, and not by an arylsulfatase as in the related species Pseudomonas aeruginosa.  (+info)

Mutational analysis of the substrate binding/catalytic domains of human M form and P form phenol sulfotransferases. (7/185)

Human monoamine (M) form and simple phenol (P) form phenol sulfotransferases (PSTs) are greater than 93% identical in their primary sequences and yet display distinct substrate specificities and other enzymatic properties. Through the generation and characterization of a series of chimeric PSTs, we have previously demonstrated two highly variable regions within their sequences to be responsible for determining their substrate phenotypes (Sakakibara, Y., Takami, Y., Nakayama, T., Suiko, M., and Liu, M.-C. (1998) J. Biol. Chem. 273, 6242-6247). By employing the site-directed mutagenesis technique, the present study aims to identify and quantitatively evaluate the specific amino acid residues critical to the substrate binding and catalysis in these two enzymes. Twelve mutated M-PSTs and seven mutated P-PSTs were generated, expressed, and purified. Enzymatic characterization showed that, of the twelve mutated M-PSTs, mutations at residues Asp-86, Glu-89, and Glu-146 resulted in a dramatic decrease in V(max)/K(m) with dopamine as substrate, being greater than 450 times for the D86A/E89I/E146A mutated M-PST. With p-nitrophenol as substrate, the V(max)/K(m) determined for the D86A/E89I/E146A-mutated M-PST increased more than 25 times and approached that determined for the wild-type P-PST. These results indicated that the concerted action of the three mutated residues (D86A, E89I, and E146A) is sufficient for the conversion of the substrate phenotype of M-PST to that of P-PST. Among the mutated P-PSTs, the I89E- and A146E-mutated P-PSTs displayed considerable deviations in V(max)/K(m) with dopamine or p-nitrophenol as substrate. No corresponding changes, however, were detected with the opposite compound as substrate. These results indicated that, in contrast to M-PST, mutations at Ala-86, Ile-89, and Ala-146 to the corresponding residues in M-PST are not sufficient for rendering the change of P-PST substrate phenotype to that of M-PST. For both M-PSTs and P-PSTs, mutations at Lys-48 or His-108 led to the loss of sulfotransferase activities, indicating their importance in the catalytic mechanism.  (+info)

In vitro bioactivation of N-hydroxy-2-amino-alpha-carboline. (8/185)

2-Amino-alpha-carboline (A alpha C) is a mutagenic and carcinogenic heterocyclic amine present in foods cooked at high temperature and in cigarette smoke. The mutagenic activity of A alpha C is dependent upon metabolic activation to N-hydroxy-A alpha C (N-OH-A alpha C); however, the metabolism of N-OH-A alpha C has not been studied. We have synthesized 2-nitro-alpha-carboline and N-OH-A alpha C and have examined in vitro bioactivation of N-OH-A alpha C by human and rodent liver cytosolic sulfotransferase(s) and acetyltransferase(s) and by recombinant human N-acetyltransferases, NAT1 and NAT2. The sulfotransferase-dependent bioactivation of N-OH-A alpha C by human liver cytosol exhibited large inter-individual variation (0.5-75, n = 14) and was significantly higher than bioactivation of N-hydroxy-2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (N-OH-PhIP). Correlation and inhibition studies suggested that the isoform of sulfotransferase primarily responsible for bioactivation of N-OH-A alpha C in human liver cytosol is SULT1A1. O-Acetyltransferase-dependent bioactivation of N-OH-A alpha C by human liver cytosol also exhibited large inter-individual variation (16-192, n = 18). In contrast to other N-hydroxy heterocyclic amines, which are primarily substrates only for NAT2, both NAT1 and NAT2 catalyzed bioactivation of N-OH-A alpha C. The rate of bioactivation of N-OH-A alpha C by both NAT1 and NAT2 was significantly higher than that for N-OH-PhIP. In rat and mouse liver cytosols, the level of sulfotransferase-dependent bioactivation of N-OH-A alpha C was similar to the level in the high sulfotransferase activity human liver cytosol. The level of O-acetyltransferase-dependent bioactivation of N-OH-A alpha C in rat liver cytosol was also comparable with that in the high acetyltransferase activity human liver cytosol. However, the level of O-acetyltransferase-dependent bioactivation of N-OH-A alpha C in mouse liver cytosol was comparable with that in the low acetyltransferase activity human liver cytosol. In contrast to N-OH-PhIP, bioactivation of N-OH-A alpha C was not inhibited by glutathione S-transferase activity; however, DNA binding of N-acetoxy-A alpha C was inhibited 20% in the presence of GSH. These results suggest that bioactivation of N-OH-A alpha C may be a significant source of DNA damage in human tissues after dietary exposure to AalphaC and that the relative contribution of each pathway to bioactivation or detoxification of N-OH-A alpha C differs significantly from other N-hydroxy heterocyclic or aromatic amines.  (+info)

The industrial solvent 2-nitropropane (2-NP) is a genotoxic hepatocarcinogen in rats. The genotoxicity of the compound in rats has been attributed to sulfotransferase-mediated formation of DNA-reactive nitrenium ions from the anionic form of 2-NP, propane 2-nitronate (P2N). Whether human sulfotransferases are capable of activating P2N is unknown. In the present study we have addressed this question by investigating the genotoxicity of P2N in various V79-derived cell lines engineered for expression of individual forms of human sulfotransferases, the phenol-sulfating and the monoamine-sulfating phenol sulfotransferases (hP-PST and hM-PST) and the human hydroxysteroid sulfotransferase (hHST). Genotoxicity was assessed by measuring the induction of DNA repair synthesis and by analyzing the formation of DNA modifications. P2N induced repair synthesis in V79-hP-PST and V79-hM-PST cells, whereas induction of repair synthesis in V79-hHST cells was negligible. P2N also resulted in the formation of ...
In recent years, significant effort has been made to identify genes that influence breast cancer risk. Because the high-penetrance breast cancer susceptibility genes BRCA1 and 2 play a role only in a small fraction of breast cancer cases, understanding the genetic risk of the majority of breast cancers will require the identification and analysis of several lower penetrance genes. The estrogen-signaling pathway plays a crucial role in the pathophysiology of breast cancer; therefore, polymorphism in genes involved in this pathway is likely to influence breast cancer risk. Our detailed analysis of gene expression profiles of estrogen- and 4-OH-tamoxifen-treated ZR75-1 breast cancer cells identified members of the sulfotransferase 1A (SULT1A) phenol sulfotransferase family as downstream targets of tamoxifen. On the basis of the induction of SULT1A by 4-OH-tamoxifen and the known inherited variability in SULT1A enzymatic activity, we hypothesized that polymorphism in sulfotransferase genes might ...
TY - JOUR. T1 - Phenolsulphotransferase in human tissue. T2 - Radiochemical enzymatic assay and biochemical properties. AU - Anderson, Robert J.. AU - Weinshilboum, R. M.. PY - 1980/4/11. Y1 - 1980/4/11. N2 - Phenolsulphotransferase (EC 2.8.2.1) (PST) is an important catecholamine and drug metabolizing enzyme. Optimal conditions have been determined for the accurate measurement of PST activity in the human platelet, human renal cortex, and human jejunum with a radiochemical microassay. 3-Methoxy-4-hydroxyphenylglycol (MHPG) and 35S-3-phosphoadenosine-5-phosphosulfate (35S-PAPS) were the substrates for the reaction. The apparent Michaelis-Menten (Km) values for MHPG with platelet, renal cortex, and jejunum were 1.09, 0.46 and 1.16 mmol/l, respectively. Apparent Km values for PAPS in the same tissues were 0.14, 0.13 and 0.21 μmol/l. The pH optimum of the reaction in all three tissues was approximately 6.2-6.8 with three different buffer systems. The coefficients of variation for the assay of ...
A full-length aryl sulfotransferase cDNA was isolated from a human liver cDNA library. It was 1155 bp long containing a coding region of 885 basepairs encoding a cytosolic protein (Mr 34178 Da) of 295 amino acids. This human cDNA shared 80% homology to the rat aryl sulfotransferase cDNA, 58% to the bovine and rat oestrogen sulfotransferase cDNAs, 53% to the rat hydroxysteroid sulfotransferase cDNA and 51% to the human liver dehydroepiandrosterone sulfotransferase cDNA over its whole 885 bp coding region. The deduced amino acid sequence of this human cDNA was 79% homologous to that of the rat aryl sulfotransferase cDNA and the putative common-substrate binding site motif GXXGXXK of the sulfotransferases has been conserved in this human amino acid sequence. At least two sizes of this human aryl sulfotransferase mRNA were detected in the human liver and lung ...
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A novel mouse liver-sulfotransferase like (mL-STL) gene was firstly identified in our laboratory with unknown physiological function. Computer assisted analysis revealed that the mL-STL gene encodes a complete cytosolic sulfotransferase (SULT) domain. SULT is a superfamily of enzymes that catalyze the transfer of a sulfate group from a cofactor, 3-phosphoadenosine 5-phosphosulfate (PAPS) to the hydroxyl group or amino group of substrates in a process called sulfonation. Different SULT family members recognize specific subsets of substrates. Dendrogram analysis indicated that the mL-STL protein shares a high amino acid sequence similarity with the SULT2A subfamily, which is known to sulfonate hydroxysteroids. This result suggests that the mL-STL protein can catalyze the SULT2A substrates. However, further study is required to confirm the substrate specificity of the mL-STL protein.. The first objective of my study is to characterize whether the mL-STL protein is a functional cytosolic SULT ...
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Complete information for SULT2B1 gene (Protein Coding), Sulfotransferase Family 2B Member 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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pep:known chromosome:VEGA66:X:20059560:20097521:1 gene:OTTMUSG00000017058 transcript:OTTMUST00000041312 gene_biotype:protein_coding transcript_biotype:protein_coding gene_symbol:Chst7 description:carbohydrate (N-acetylglucosamino) sulfotransferase 7 ...
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Human scalp skin high speed supernatants were used to test whether minoxidil sulfotransferase (MNX-ST) and phenol sulfotransferase (PST) activities were present. Platelet homogenates from the same skin donors were used to test whether levels of sulfotransferase activities in the blood platelet would reflect levels of the enzyme activities in skin. Dopamine, p-nitrophenol and minoxidil were used as substrates for skin and platelet thermolabile (TL PST), thermostable (TS PST) and MNX-ST activities, respectively. Biochemical properties of each skin enzyme were the same as the platelet enzymes with respect to apparent Km values for substrates, pH optima, thermal stabilities and responses to inhibition by 2,6-dichloro-4-nitrophenol (DCNP). An unexpected finding was that skin and platelet MNX-ST thermal stabilities and responses to DCNP were more similar to TL PST than to TS PST, the enzyme reported to be responsible for MNX-ST activity. There were significant positive correlations of platelet ...
TY - JOUR. T1 - L-DOPA biotransformation. T2 - Correlations of dosage, erythrocyte catechol O-methyltransferase and platelet SULT1A3 activities with metabolic pathways in Parkinsonian patients. AU - Dousa, M. K.. AU - Weinshilboum, Richard M. AU - Muenter, M. D.. AU - Offord, K. P.. AU - Decker, P. A.. AU - Tyce, G. M.. PY - 2003/8/1. Y1 - 2003/8/1. N2 - The objectives of this study were to determine (1) the effects of dose and drug absorption on pathways of biotransformation of L-DOPA in Parkinsonian patients treated with Sinemet, and (2) the extent to which genetically-determined variations in the activities of erythrocyte catechol O-methyltransferase and/or platelet phenol sulfotransferase might be reflected in individual differences in L-DOPA metabolism. In the 19 patients studied, there were negative correlations between dosage or absorption and extent of O-methylation and of sulfation of L-DOPA or its metabolites. Levels of activity for erythrocyte COMT were also reflected in individual ...
Then I checked out yet another gluten-free cookbook from the library- always trying to find new ones for new recipe ideas. This one was The Kid Friendly ADHD & Autism Cookbook by Pamela J. Compart, M.D. and Dana Laake, R.D.H., M.S., L.D.N. Yet again I found another little segment in this book describing Brian and lo and behold, it was titled, "Phenol Intolerance- Phenol Sulfotransferase (PST) Deficiency".. This book was able to describe the science to me in better terms for me to understand it. As a lot of scientists, and certainly a lot of parents, believe most children with ADHD and autism have many inefficiencies in metabolic enzyme function and deficiencies in nutrients. Enzymes depend on nutrients to function properly in our bodies. When the enzymes are "lazy" a sort of traffic jam happens in their bodies. Metabolites that result from normal metabolic pathways get backed up. The "traffic" starts causing problems on other enzyme pathways. In the body, the only way to solve this gridlock is ...
Accepted name: estrone sulfotransferase. Reaction: 3-phosphoadenylyl sulfate + estrone = adenosine 3,5-bisphosphate + estrone 3-sulfate. Glossary: 3-phosphoadenylyl sulfate = PAPS. Other names: 3-phosphoadenylyl sulfate-estrone 3-sulfotransferase; estrogen sulfotransferase; estrogen sulphotransferase; oestrogen sulphotransferase; 3-phosphoadenylylsulfate:oestrone sulfotransferase. Systematic name: 3-phosphoadenylyl-sulfate:estrone 3-sulfotransferase. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-06-6. References:. 1. Adams, J.B. and Poulos, A. Enzymic synthesis of steroid sulphates. 3. Isolation and properties of estrogen sulphotransferase of bovine adrenal glands. Biochim. Biophys. Acta 146 (1967) 493-508. [PMID: 4965224]. 2. Rozhin, J., Zemlicka, J. and Brooks, S.C. Studies on bovine adrenal estrogen sulfotransferase. Inhibition and possible involvement of adenine-estrogen stacking. J. Biol. Chem. 252 (1967) 7214-7220.. 3. Adams, J.B., Ellyard, ...
Sulfotransferase that utilizes 3-phospho-5-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk (By similarity).
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iodothyronine sulfotransferase: hepatic enzyme involved in sulfation of thyroid hormone; SULT1B1 catalyzes the biotransformation of a large number of endogenous compounds such as NEUROTRANSMITTERS, STERIODS, BILE ACIDS, and tTHYROID HORMONES, as well as drugs and XENOBIOTICS; RefSeq NM_014465 (human)
Drug-drug interactions associated with EE2 therapy have been primarily studied in regard to the cytochromes P450. Few studies investigating interactions with the SULTs or other major conjugating enzyme systems have been reported. The inhibition of SULT1A1 at low nanomolar concentrations of EE2 while allowing for EE2 sulfation at higher concentrations suggests a new paradigm for investigating and understanding drug-drug interactions involving SULT1A1 and possibly other isoforms. SULT1A1 is the major xenobiotic sulfating isoform in liver and is widely expressed throughout the body (Hempel et al., 2007); however, its interactions in EE2 therapy are not well studied. The potent inhibition of SULT1A1 was unexpected and indicates that more attention should be paid to sulfation of both drugs and xenobiotics during concurrent therapy with EE2-containing contraceptives. Lack of sulfation activity at the inhibitory concentrations also suggests a relatively long duration of inhibition. Combined with the ...
View mouse Chst15 Chr7:132235780-132317228 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
Sigma-Aldrich offers abstracts and full-text articles by [Xiaojuan Chai, Yan Guo, Mengxi Jiang, Bingfang Hu, Zhigang Li, Jie Fan, Meihong Deng, Timothy R Billiar, Heidi R Kucera, Nilesh W Gaikwad, Meishu Xu, Peipei Lu, Jiong Yan, Haiyan Fu, Youhua Liu, Lushan Yu, Min Huang, Su Zeng, Wen Xie].
Hydroxysteroid sulfotransferase 2B1b (SULT2B1b) sulfates cholesterol and oxysterols. Hepatic oval cells (HOCs), thought to be progenitor cells, can be triggered in chemically injured livers. The...
Looking for online definition of carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 14 in the Medical Dictionary? carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 14 explanation free. What is carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 14? Meaning of carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 14 medical term. What does carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 14 mean?
... General Systematic name Sulfuryl chloride Other names Sulfonyl ChlorideSulfuric chloride Molecular formula SO2Cl2 CAS
Dermatan 4-sulfotransferase (EC 2.8.2.35, dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase, dermatan-4-sulfotransferase-1, dermatan-4-sulfotransferase 1, D4ST-1, dermatan N-acetylgalactosamine 4-O-sulfotransferase, CHST14 protein, CHST14) is an enzyme with systematic name 3-phospho-5-adenylyl sulfate:(dermatan)-N-acetyl-D-galactosamine 4-sulfotransferase. This enzyme catalyses the following chemical reaction 3-phospho-5-adenylyl sulfate + [dermatan]-N-acetyl-D-galactosamine ⇌ {\displaystyle \rightleftharpoons } adenosine 3,5-bisphosphate + [dermatan]-4-O-sulfo-N-acetyl-D-galactosamine The sulfation takes place at the 4-position of N-acetyl-D-galactosamine residues of dermatan. Evers, M.R.; Xia, G.; Kang, H.G.; Schachner, M.; Baenziger, J.U. (2001). "Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase". J. Biol. Chem. 276: 36344-36353. doi:10.1074/jbc.M105848200. PMID 11470797. Mikami, T.; Mizumoto, S.; Kago, N.; Kitagawa, ...
Estrogen sulfotransferase (EST) is a cytosolic enzyme that catalyzes the sulfonation of estrogens at the 3-hydroxyl position by use of 3′-phosphoadenosine-5′-phosphosulfate as an activated sulfate donor. Although largely known and studied as a phase II metabolic enzyme with prominent expression in the liver, the high substrate specificity of EST (with a highVmax/Km value for estrogen) suggests that expression of the enzyme in extrahepatic, estrogen target tissues, such as the breast epithelium, may constitute an effective mechanism for local estrogen regulation as well. In this study, we have evaluated the physiological significance of EST expression by cDNA transfection studies with use of the estrogen-dependent MCF-7 breast cancer cell line as a model system. We show that expression of EST in MCF-7 cells effectively reduces the cells response to physiological concentrations of estradiol (10 nM) by up to 70% as determined in an estrogen-responsive reporter gene assay. In addition, we ...
2 Answers to Sulfuryl chloride, SO 2 Cl 2 , decomposes when heated: SO 2 Cl 2 (g) ? SO 2 (g) + Cl 2 (g) In an experiment, the initial concentration of sulfuryl chloride was 0.0248 mol/L. The reaction is first order, and the rate constant is 2.2 x 10 -5 s -1 . What is the concentration of SO 2 Cl 2 after 4.5 hr? - 117134
Bioactivation of 3-n-butylphthalide via sulfation of its major metabolite 3-hydroxy-NBP: mediated mainly by sulfotransferase 1A1. - Xingxing Diao, Xiaoyan Pang, Cen Xie, Zitao Guo, Dafang Zhong, Xiaoyan Chen
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Cholesterol sulfate has been shown to be a normal constituent of blood platelets and to modulate platelet function.11 For example, it potentiates ADP- and thrombin-induced platelet aggregation as well as serotonin secretion. These effects are specific for cholesterol sulfate and require both the sterol ring structure as well as the sulfate moiety.11 Furthermore, cholesterol sulfate modulates arachidonic acid metabolism while potentiating arachidonic acid-induced platelet aggregation, effects that are, in part, explained by changes in calcium flux.17 It has also been shown that platelets will adhere to cholesterol sulfate but not to cholesterol, other cholesterol esters, or other steroid sulfates under flow conditions similar to those seen in arteries.12. It is now appreciated that SULT2B1b is the physiological cholesterol sulfotransferase.21 SULT2B1b is selectively expressed in specific tissues, where it is known that cholesterol sulfate plays an important physiological role, eg, skin.25 We now ...
glycolithocholate sulfate = N-(3α-sulfooxy-5β-cholan-24-oyl)glycine. Other name(s): BAST I; bile acid:3-phosphoadenosine-5-phosphosulfate sulfotransferase; bile salt:3phosphoadenosine-5-phosphosulfate:sulfotransferase; bile acid sulfotransferase I; glycolithocholate sulfotransferase. Systematic name: 3-phosphoadenylyl-sulfate:glycolithocholate sulfotransferase. Comments: The formation of sulfate esters of bile acids is an essential step in the prevention of toxicity by monohydroxy bile acids in many species [3]. This enzyme is both a bile salt and a 3-hydroxysteroid sulfotransferase. In addition to the 5β-bile acid glycolithocholate, deoxycholate, 3β-hydroxy-5-cholenoate and dehydroepiandrosterone (3β-hydroxyandrost-5-en-17-one) also act as substrates [see also EC 2.8.2.2 (alcohol sulfotransferase) and EC 2.8.2.34 (glycochenodeoxycholate sulfotransferase)]. May be identical to EC 2.8.2.2 [3].. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: ...
Alterations in protein synthesis in primary cultured rat liver parenchymal cells were examined after their exposure to the potent carcinogens, polychlorinated biphenyl (PCB) congeners. Co-planar PCB congeners (3,4,5,3′,4′-PCB and 3,4,5,3′,4′,5′-PCB) (10 nM) induced a protein, the Mr of which was 25,000 (25 k protein) under denaturing conditions. However, non-co-planar PCB congeners and several xenobiotics, which induce microsomal proteins, did not induce the 25 k protein. By using immunoblotting, the 25 k protein was identified as glutathione S-transferase P-form (GST-P, 7-7, EC 2.5.1.18).. ...
The formation of sulfate esters of bile acids is an essential step in the prevention of toxicity by monohydroxy bile acids in many species [3]. This enzyme is both a bile salt and a 3-hydroxysteroid sulfotransferase. In addition to the 5beta-bile acid glycolithocholate, deoxycholate, 3beta-hydroxy-5-cholenoate and dehydroepiandrosterone (3beta-hydroxyandrost-5-en-17-one) also act as substrates [see also EC 2.8.2.2 (alcohol sulfotransferase) and EC 2.8.2.34 (glycochenodeoxycholate sulfotransferase)]. May be identical to EC 2.8.2.2 [3 ...
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The Biocidal Products Committee (BPC) is part of the European Chemicals Agency (ECHA).. BPC opinion pursuant to Article 75 (1)(g) on sulfuryl fluoride in PTs 8 and 18.. The request concerns the monitoring data from remote tropospheric air, which the authorisation holder submitted to the European Commission to comply with the decisions on the approval of sulfuryl fluoride (PTs 8 and 18) under the Biocidal Products Directive (BPD). The BPC was asked to give an opinion by the European Commission on whether the previous conclusions with respect to the global warming potential of sulfuryl fluoride under the BPD are still valid. The conclusion of the BPC was that the global warming potential based on the monitoring data submitted is higher than previously estimated. The BPC recommended to continue monitoring and that the global warming potential has to be considered under the renewal process of sulfuryl fluoride.. See original. ...
Methyl Furfuryl Disulfide 57500-00-2 NMR spectrum, Methyl Furfuryl Disulfide H-NMR spectral analysis, Methyl Furfuryl Disulfide C-NMR spectral analysis ect.
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Sulfation or sulfurylation (not to be confused with sulfonation) in biochemistry is the enzyme-catalyzed conjugation of a sulfo group (not a sulfate or sulfuryl group) to another molecule. This biotransformation involves a sulfotransferase enzyme catalyzing the transfer of a sulfo group from a donor cosubstrate, usually 3-phosphoadenosine-5-phosphosulfate (PAPS), to a substrate molecules hydroxyl or amine. Sulfation is involved in a variety of biological processes, including detoxification, hormone regulation, molecular recognition, cell signaling, and viral entry into cells. It is among the reactions in phase II drug metabolism, frequently effective in rendering a xenobiotic less active from a pharmacological and toxicological standpoint, but sometimes playing a role in the activation of xenobiotics (e.g. aromatic amines, methyl-substituted polycyclic aromatic hydrocarbons). Another example of biological sulfation is in the synthesis of sulfonated glycosaminoglycans, such as heparin, heparan ...
The report generally describes sulfuryl chloride fluoride, examines its uses, production methods, patents. SULFURYL CHLORIDE FLUORIDE market situation
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Both phosphoryl and sulfuryl transfers are ubiquitous in biology, being involved in a wide range of processes, ranging from cell division to apoptosis. Additionally, it is becoming increasingly clear that enzymes that can catalyze phosphoryl transfer can often cross-catalyze sulfuryl transfer (and vice versa). However, while there have been extensive experimental and theoretical studies performed on phosphoryl transfer, the body of available research on sulfuryl transfer is comparatively much smaller. The present work presents a direct theoretical comparison of p-nitrophenyl phosphate and sulfate monoester hydrolysis, both of which are considered prototype systems for probing phosphoryl and sulfuryl transfer, respectively. Specifically, free energy surfaces have been generated using density functional theory, by initial geometry optimization in PCM using the 6-31+G* basis set and the B3LYP density functional, followed by single-point calculations using the larger 6-311+G** basis set and the ...
Sulfotransferase that utilizes 3-phospho-5-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues and O-linked sugars of mucin-type acceptors. Acts on the non-reducing terminal GlcNAc of short carbohydrate substrates. However, it does not transfer sulfate to longer carbohydrate substrates that have poly-N-acetyllactosamine structures. Has no activity toward keratan. Not involved in generating HEV-expressed ligands for SELL. Its substrate specificity may be influenced by its subcellular location ...
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The Fano sequential decoding algorithm is brief ly described. A computer program (FSD) for executing the algorithm on a simulated binary symmetric channel is discussed and certain re sults obtained with the program are reported. The major results are: good values of the de coding parameters, d(o) and T(o), are found and their adjustment is not critical; the tail of the cumulative distribution function of the number of computations per information bit appears to obey a Pareto law; the behavior of the waiting line in the buffer at the receiver input is pre dicted by extrapolating on the Pareto behavior of the number of computations. (Author)TDR63 88
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The adrenal steroid dehydroepiandrosterone (DHEA) and its sulphate ester, DHEAS are the most abundant circulating steroid hormones in humans. Uncongugated DHEA predominately exerts its effects via its downstream conversion to active sex steroids in peripheral target tissues. In contrast the conversion of DHEAS to androgens first requires cleavage of the sulfate group, catalysed by the microsomal enzyme steroid sulfatase (STS). Conversely, DHEA is converted to inactive DHEAS by the activity of the cytosolic enzyme DHEA sulphotransferase (SULT2A1). However, in addition, evidence is growing that DHEA and DHEAS can have specific, direct effects. In this thesis, I have demonstrated that abrogation of DHEA metabolism can result in the manifestation of pathophysiological conditions. SULT2A1 requires 3-phosphoadenosine-5-phosphosulfate (PAPS) for catalytic activity. I have identified compound heterozygous mutations in the gene encoding human PAPS synthase 2 (PAPSS2) in a girl with androgen excess and ...
TY - JOUR. T1 - CYP2D6 genotype, antidepressant use, and tamoxifen metabolism during adjuvant breast cancer treatment. AU - Diasio, Robert B. PY - 2006/1. Y1 - 2006/1. UR - http://www.scopus.com/inward/record.url?scp=30744478024&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=30744478024&partnerID=8YFLogxK. U2 - 10.1016/S1043-321X(05)80305-4. DO - 10.1016/S1043-321X(05)80305-4. M3 - Article. VL - 16. SP - 372. EP - 374. JO - Breast Diseases. JF - Breast Diseases. SN - 1043-321X. IS - 4. ER - ...
It was found that a fluoro derivative can be produced by reacting a hydroxy derivative with sulfuryl fluoride (SO2F2) in the presence of an organic base or in the presence of an organic base and a salt or complex comprising an organic base and hydrogen fluoride. According to the present production process, it is not necessary to use perfluoroalkanesulfonyl fluoride, which is not preferable in industrial use, and it is possible to advantageously produce optically-active fluoro derivatives, which are important intermediates of medicines, agricultural chemicals and optical materials, specifically 4-fluoroproline derivatives, 2-deoxy-2-fluorouridine derivatives, optically-active α-fluorocarboxylate derivatives, and the like, even in a large scale ...
Complete information for CHST14 gene (Protein Coding), Carbohydrate Sulfotransferase 14, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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1998), SULT1A1 shows clearly the highest activity towards 4-nitrophe- nol and therefore is likely to mediate the sulphonation of 1,2,3,4-tetraisoquinoline. Antiviral. B.
The protein encoded by this gene belongs to the sulfotransferase 2 family. It is localized to the golgi membrane, and catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin and desulfated dermatan sulfate. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage, and is distributed on the surfaces of many cells and extracellular matrices. Alternatively spliced transcript variants differing only in their 5 UTRs have been found for this gene.
Wang, X.-R., Qu, Z.-Q., Li, X.-D., Liu, H.-L., He, P., Fang, B.-X., Xiao, J., Huang, W. and Wu, M.-C. (2010), Activity of sulfotransferase 1A1 is dramatically upregulated in patients with hepatocellular carcinoma secondary to chronic hepatitis B virus infection. Cancer Science, 101: 412-415. doi: 10.1111/j.1349-7006.2009.01404.x ...
1G3M: Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase.
2C72: Functional Role of the Aromatic Cage in Human Monoamine Oxidase B: Structures and Catalytic Properties of Tyr435 Mutant Proteins
TY - JOUR. T1 - Indirect regulation of human dehydroepiandrosterone sulfotransferase family 1A member 2 by thyroid hormones. AU - Huang, Ya Hui. AU - Lee, Yi Chih. AU - Tai, Pei Ju. AU - Yen, Chun Che. AU - Liao, Chu Yu. AU - Chen, Wei Jan. AU - Liao, Cheng Jung. AU - Cheng, Wan Li. AU - Chen, Ruey Nan. AU - Wu, Sheng Ming. AU - Wang, Chia Siu. AU - Lin, Kwang Huei. PY - 2006/5. Y1 - 2006/5. N2 - Thyroid hormone, T3, regulates cell metabolism, differentiation, and development. cDNA microarrays were performed to study the mechanism of target gene regulation after T3 treatment in a thyroid hormone receptor-α (TRα)-overexpressing hepatoma cell line (HepG2-TRα). The differentially expressed target genes are several metabolic enzymes, including dehydroepiandrosterone-sulfotransferase family 1A member 2 (SULT2A1). Enzyme SULT2A1 was elevated roughly 5-fold at the protein level and 9-fold increase at the mRNA level after 48 h T3 treatment in HepG2-TRα cells. Cycloheximide inhibited T3-induced ...
THE MORNING JOURNAL. COLUMBUS, OHIO: THURSDAY NOVEMBER 7, 1867. NO. 100. VOL. XXX. . -. - . . " i HEADING MATTER OTH EVERY PAKE TELEGRAPHIC REPORTED FOR THE JOURNAL. FOREIGN NEWS. By Atlantio Telegraph. east of Exeter, where the premises of the corn dealers have been burned. Ax Minster contains the well known carpet factories, with buildings for the manufacture r.f wnnlpn r.loth and cloves, and has very determined population workingmen. called out aud WASHINGTON. NEWS. Statement of Public Debt. Washington, Nov. 0. The followinz Is a statement of the public rieht. nn thfi 1st of November : Debt bearing f min int.M-pst,. S nor cent, bonds. $1!8,845,350; terminal P . six pe7c n bomls of 1807, $1,469,004.185 ; next day. The local militia has been cent of mh mmfi0O . six j piaceu uuuur iuun " per cent, bonds, o-aus, i,su(,owo,iw! xiavj The 103d O. V. I. Is to have a reunion at Cleveland on Thanksgiving day. Snow fell to the depth of three or four Inches at Elyria, last week but melted off New ...
12-Hydroxyjasmonate, also known as tuberonic acid, was first isolated from Solanum tuberosum and was shown to have tuber-inducing properties. It is derived from the ubiquitously occurring jasmonic acid, an important signaling molecule mediating diver
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Kobashi K, Kim D-H & Morikawa T (1987). "A novel type of arylsulfotransferase". J. Protein Chem. 6: 237-244. doi:10.1007/ ... Kim DH, Konishi L, Kobashi K (1986). "Purification, characterization and reaction mechanism of novel arylsulfotransferase ... Other names in common use include arylsulfate-phenol sulfotransferase, arylsulfotransferase, ASST, arylsulfate sulfotransferase ...
Other names in common use include aryl sulfotransferase IV, and L-tyrosine methyl ester sulfotransferase. Duffel MW, Jakoby WB ... Sekura RD, Jakoby WB (1981). "Aryl sulfotransferase IV from rat liver". Arch. Biochem. Biophys. 211 (1): 352-9. doi:10.1016/ ... 1981). "On the mechanism of aryl sulfotransferase". J. Biol. Chem. 256 (21): 11123-7. PMID 6945304. Mattock P, Jones JG (1970 ...
Bernier F, Leblanc G, Labrie F, Luu-The V (1994). "Structure of human estrogen and aryl sulfotransferase gene. Two mRNA species ... 1993). "Identification of two human brain aryl sulfotransferase cDNAs". Biochem. Biophys. Res. Commun. 195 (1): 120-7. doi: ...
"Structure of human estrogen and aryl sulfotransferase gene. Two mRNA species issued from a single gene". J Biol Chem. 269 (45 ...
1998). "Localisation of aryl sulfotransferase expression in human tissues using hybridisation histochemistry and ... Zhu X, Veronese ME, Sansom LN, McManus ME (1993). "Molecular characterisation of a human aryl sulfotransferase cDNA". Biochem. ... 1993). "Identification of two human brain aryl sulfotransferase cDNAs". Biochem. Biophys. Res. Commun. 195 (1): 120-7. doi: ...
Zhu X, Veronese ME, Iocco P, McManus ME (1996). "cDNA cloning and expression of a new form of human aryl sulfotransferase". Int ... 1998). "Localisation of aryl sulfotransferase expression in human tissues using hybridisation histochemistry and ...
Cytochrome P450 monooxygenase, aryl sulfotransferase, glutathione S-transferase, UDP-glucuronosyltransferase, UDP- ...
... aryl sulfotransferase EC 2.8.2.2: alcohol sulfotransferase EC 2.8.2.3: amine sulfotransferase EC 2.8.2.4: estrone ...
... aryl sulfotransferase MeSH D08.811.913.817.500 --- sulfurtransferases MeSH D08.811.913.817.500.500 --- thiosulfate ...
An aryl sulfotransferase (EC 2.8.2.1) is an enzyme that transfers a sulfate group from phenolic sulfate esters to a phenolic ... arylsulfotransferase, dopamine sulfotransferase, p-nitrophenol sulfotransferase, phenol sulfokinase, ritodrine sulfotransferase ...
Aryl sulfotransferase. *Asialoglycoprotein receptor. *Aspartate carbamoyltransferase. *Aspartate-semialdehyde dehydrogenase. * ...
A full-length aryl sulfotransferase cDNA was isolated from a human liver cDNA library. It was 1155 bp long containing a coding ... Zhu X.Y., Veronese M.E., Sansom L.N. and Mcmanus M.E. (1993) Molecular Characterization of a Human Aryl Sulfotransferase cDNA. ... The deduced amino acid sequence of this human cDNA was 79% homologous to that of the rat aryl sulfotransferase cDNA and the ... Molecular Characterization of a Human Aryl Sulfotransferase cDNA Journal name Biochemical and Biophysical Research ...
An aryl sulfotransferase (EC 2.8.2.1) is an enzyme that transfers a sulfate group from phenolic sulfate esters to a phenolic ... arylsulfotransferase, dopamine sulfotransferase, p-nitrophenol sulfotransferase, phenol sulfokinase, ritodrine sulfotransferase ...
INFLUENCE OF PHENYLALANINES 77 AND 138 ON THE STEREOSPECIFICITY OF ARYL SULFOTRANSFERASE IV. Jonathan J. Sheng, Atmaja Saxena ... INFLUENCE OF PHENYLALANINES 77 AND 138 ON THE STEREOSPECIFICITY OF ARYL SULFOTRANSFERASE IV. Jonathan J. Sheng, Atmaja Saxena ... INFLUENCE OF PHENYLALANINES 77 AND 138 ON THE STEREOSPECIFICITY OF ARYL SULFOTRANSFERASE IV. Jonathan J. Sheng, Atmaja Saxena ... Aryl sulfotransferase (AST) IV (also named tyrosine-ester sulfotransferase and ST1A1) is a major phenol sulfotransferase in the ...
Localisation of aryl sulfotransferase expression ... - Semantic Scholar. pdfs.semanticscholar.org. Windmill a. , Astrid ...
aryl sulfotransferase activity Source: UniProtKB-EC. Complete GO annotation on QuickGO .... GO - Biological processi. * ...
aryl sulfotransferase activity Source: Reactome. *identical protein binding Source: IntAct ,p>Inferred from Physical ...
... aryl sulfotransferase [EC:2.8.2.1] K07410 CYP1B1; cytochrome P450 family 1 subfamily B polypeptide 1 [EC:1.14.14.1] K07413 ...
aryl sulfotransferase activity. TAS. --. GO:0004304. estrone sulfotransferase activity. TAS. --. GO:0005515. protein binding. ...
Aryl sulfotransferase 1A3/1A4 antibody. *Aryl sulfotransferase antibody. *Catecholamine Sulfating Phenol Sulfotransferase ...
Arylsulfotransferase / genetics* * Case-Control Studies * Colon / metabolism * Colorectal Neoplasms / epidemiology * Colorectal ...
Springer Handbook of Enzymes provides data on enzymes sufficiently well characterized. It offers concise and complete descriptions of some 5,000 enzymes and their application areas. Data sheets are ar
Aryl sulfotransferase activity. Gene Name. assT. Uniprot ID. A0A0H2Z368. Uniprot Name. Arylsulfate sulfotransferase AssT. ...
Aryl sulfotransferase 1. *Cytosolic Sulfotransferase 1A1. *EC 2.8.2. *EC 2.8.2.1. *HAST1/HAST2 ...
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Aryl sulfotransferase activity. Gene Name. assT. Uniprot ID. A0A0H2Z368. Uniprot Name. Arylsulfate sulfotransferase AssT. ...
Arylsulfotransferase (metabolism) *Benzofurans (metabolism, pharmacokinetics, toxicity) *Biotransformation. *Cell Survival ( ...
Cytosolic Aryl sulfotransferase 4A1 interacts with the peptidyl prolyl cis-trans isomerase Pin1. ...
Keywords: Arylsulfotransferase, 3-CYANO-7-HYDROXYCUMARIN, TRANSFERASE. Deposited on 2011-10-06, released 2011-11-16. The last ...
Kobashi K, Kim D-H & Morikawa T (1987). "A novel type of arylsulfotransferase". J. Protein Chem. 6: 237-244. doi:10.1007/ ... Kim DH, Konishi L, Kobashi K (1986). "Purification, characterization and reaction mechanism of novel arylsulfotransferase ... Other names in common use include arylsulfate-phenol sulfotransferase, arylsulfotransferase, ASST, arylsulfate sulfotransferase ...
Keywords: aryl sulfotransferase; neurolipins; metabolism; liver; nervous system Comparison of redox state of cells of tatar ...
Transcriptional regulation of rat hepatic aryl sulfotransferase (SULT1A1) gene expression by glucocorticoids.. *Zhengbo Duanmu ... the effects of glucocorticoid and antiglucocorticoid hormones on rat hepatic hydroxysteroid sulfotransferase-a and aryl sulfotransferase ...
SULT1A2; sulfotransferase family, cytosolic, 1A, phenol-preferring, member 2; STP2; sulfotransferase 1A2; HAST4; P-PST 2; aryl sulfotransferase ...
Using a general aryl sulfotransferase riboprobe (HAST1), we have demonstrated marked sulfotransferase expression in the human ...
Aryl sulfotransferase; Phenol sulfotransferase; Phenol/aryl sulfotransferase Product Gene Name Sult1a1 recombinant protein. [ ... Aryl sulfotransferase; Phenol sulfotransferase; Phenol/aryl sulfotransferase; mSTp1; ST1A4; Sulfokinase. Protein Family ...