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Adenosine 3 -phosphate-5 -phosphosulfate

It has been proposed that 8-aminodcoxyguanosinc is formed from the nitronate tautomer of 2-nitropropane either by base nitrosation followed by reduction, or via an enzyme-mediated conversion of the nitronate anion to hydroxyiam ine-O-sulfonate or acetate, which yields the highly reactive nitrenium ion NHj (Sodum et al., 1993). Sodum et al. (1994) have provided evidence for the activation of 2-nitropropane to an aminating species by rat liver aryl sulfotransferase in vitro and in vivo. Pretreatment of rats with the aryl sulfotransferase inhibitors pentachlorophenol or 2,6-dichloro-4-nitrophenol significantly decreased the levels of nucleic acid modifications produced in the liver by 2-nitropropane treatment. Partially purified rat liver aryl sulfotransferase activated 2-nitropropane and its nitronate at neutral pH to a reactive species that aminated guanosine at the position. This activation was dependent on the presence of the enzyme, its specific cofactor adenosine 3 -phosphate 5 -phosphosulfate, and mercaptoethanol. It was inhibited... [Pg.1089]

The most significant instance of addition of a sulfur-containing group is the phase II conjugation to sulfate of a xenobiotic compound or its phase I metabolite (see Section 7.4.3) by the action of adenosine 3 -phosphate-5 -phosphosulfate, a sulfotransferase enzyme that acts as a sulfating agent ... [Pg.364]

In a typical procedure to study sulfation reactions (Tabrett 2003) the reaction mixtures consists of a 6.25 mM potassium phosphate buffer (pH 7.4), containing 60 pM adenosine 3 -phosphate 5 -phosphosulfate (PAPS) as a cofactor, 75 pg liver cytosolic protein and 0.125-100 pM substrate (4-nitrophenol in the... [Pg.515]

Sulfotransferase catalyzes the transfer of sulfate from the donor molecule adenosine-3 -phosphate-5 -phosphosulfate (PAPS) to an acceptor, /3-naphthol, to form the reaction product /3-naphthol sulfate. [Pg.375]

Nucleoside 2 (or 3 ),5 -diphosphates have been isolated by degradation of certain coenzymes, as well as from hydrolyzates of nucleic acids. Adenosine 3, 5 -diphosphate (see p. 320) has been isolated by enzymic hydrolysis of coenzyme A and from active sulfate (adenosine 3 -phosphate 5 -phosphosulfate). Adenosine 2, 5 -diphosphate was shown to be present in the adenylic acid moiety of the coenzyme adenine-nicotinamide dinucleotide phosphate which, by treatment with a 5 -nucleotidase from potatoes, is converted into adenosine 2 -phosphate. Adenosine 3, 5 -di-phosphate is reported to play a role as a cofactor in the bioluminescence of Renilla reniformis (pansy) Ribonucleic acid carrying a terminal 5 -phos-phate group yields ribonucleoside 3, 5 -diphosphates on digestion with phosphoesterases. ... [Pg.321]

Hjelle, J. J., Hazelton, G. A., and Klaassen, C. D. (1985) Acetaminophen decreases adenosine 3 -phosphate 5 -phosphosulfate and uridine diphosphoglucuronic acid in rat liver. Drug Metab. Dispos. 13, 35 41. [Pg.95]

A pathway first outlined in detail by Davies et al. (1966) has been examined in a number of tissues. Davies et al. (1966) used Euglena gracilis and showed that cysteic acid could act as a precursor of the sulfolipid. Incorporation from 801 was reduced in the presence of molybdate, which was thought to implicate adenosine-3 -phosphate 5 -phosphosulfate (PAPS). As a result of these experiments (see Table II), Davies et al. (1966) suggested a pathway involving formation of the sulfonic acid grouping by the reaction of PAPS with phosphoenolpyruvate. This reaction would be followed by a number of interconversions and, finally, by an aldol condensation with dihy-droxyacetone phosphate. [Pg.304]

The adenosine-3 -phosphate-5 -phosphosulfate (PAPS) generating system could be located in the 105,000 g supernatant of rat brain, whereas the Gal-Cer sulfotransferase remained particle bound. Substrate may be Gal-Cer or lactosyl ceramide. Sulfatides of kidney show a higher metabolic turnover than those in brain. Water-soluble sulfatide, discovered in the 105,000 g supernatant of a brain homogenate, was found to be complexed to certain specific proteins (Hersch-kowitz et al., 1968). It was postulated that this might represent a transport form from the site of biosynthesis to the myelin. [Pg.270]

Capasso JM, Hirschberg CB. Effect of nucleotides on translocation of sugar nucleotides and adenosine 3 -phosphate 5 -phosphosulfate into Golgi apparatus vesicles. Biochim. Biophys. Acta 1984 777 133-139. [Pg.1155]

Mandon EC, Milla ME, Kempner E, Hirschberg CB. Purification of the Golgi adenosine 3 -phosphate 5 -phosphosulfate transporter, a homodimer within the membrane. Proc. Natl Acad. Sci. U.S.A. 1994 97 10707-10711. [Pg.1157]

Adenosine 5 -phosphosulfate was separated from ATP and other adenine nucleotides by chromatography on a Synchropak AX-100 column (4.1 mm x 250 mm). The mobile phase contained 0.1 M sodium phosphate buffer (pH 7.3) and 0.8 M NaHC03. The effluent profile was obtained by monitoring at 254 nm. [Pg.375]

A.7.1 Esterification of Acids using Carbodiimides. The formation of anhydrides from carboxylic acids, thiocarboxylic acids, sulfonic acids and phosphorous acids are discussed in Section 2.4.S.2. In this section only special cases of anhydride formation are described. Mixed anhydrides of amino acids and adenylic acid are produced from the corresponding acids using DCC as the condensation agent. ° Mixed anhydrides not containing amino acids, such as butyryl adenate, adenosine 5 -phosphosulfate and p-nitrophenyl-thymidine-5-phosphate are also obtained. [Pg.113]

Fig. 31.41 The sulfoconjugation reaction example of 4-nitrophenol as acceptor substrate. Step 1, PAPS formation from adenosine 5 -phosphosulfate (APS) step 2, sulfate conjugation with the subsequent release of 3 -phosphoadenosine 5 -phosphate (PAP) step 3, possible hydrolysis of the sulfoconjugate by arylsulfatases. Fig. 31.41 The sulfoconjugation reaction example of 4-nitrophenol as acceptor substrate. Step 1, PAPS formation from adenosine 5 -phosphosulfate (APS) step 2, sulfate conjugation with the subsequent release of 3 -phosphoadenosine 5 -phosphate (PAP) step 3, possible hydrolysis of the sulfoconjugate by arylsulfatases.
Sulfotransferases catalyze the transfer of a sulfate (i.e., sulfonate, SO3) group from an activated donor onto the hydroxyl or less commonly the amino group of the acceptor molecule. The activated donor is invariably 3 phosphoadenosine 5 phosphosulfate (PAPS) [4]. PAPS is synthesized from ATP and S04 by the sequential action of ATP sulfurylase, which generates adenosine 5 phosphosulfate (APS), and APS kinase, which transfers a phosphate from ATP to APS. Chlorate, a drug which has been extremely useful for implicating the importance of sulfation... [Pg.1362]

In a first step ATP and sulfate react to form adenosine-5 -phospho-sulfate (APS), a sulfate analog of ADP, and inorganic pyrophosphate. This reversible reaction is pulled by inorganic pyrophosphatase. The sulfurylase is not specific for sulfate, but also reacts with several other anions. In a second step, APS is phosphorylated in the 3 position in an irreversible kinase reaction in which ATP is the phosphate donor. The products of the kinase reaction are ADP and 3 -phosphoadenosine-5 -phosphosulfate (PAPS). ... [Pg.331]

Abbreviations NADPH, p-nicotinamide adenine dinucleotide phosphate reduced form NAD, p-nicotinamide adenine dinucleotide FAD, flavin adenine dinucleotide FMN, flavin mononucleotide ATP, adenosine triphosphate PAPS, 3 -phosphoadenosine 5 -phosphosulfate UDP, uridine diphosphate UDPGA, uridine diphosphate-glucuronic acid. [Pg.334]

Adeno8ine-3 -phosphate-5 phosphosulfate (PAPS) Adenosine-S -phospho-selenate... [Pg.509]


See other pages where Adenosine 3 -phosphate-5 -phosphosulfate is mentioned: [Pg.289]    [Pg.155]    [Pg.155]    [Pg.231]    [Pg.26]    [Pg.418]    [Pg.439]    [Pg.318]    [Pg.340]    [Pg.454]    [Pg.318]    [Pg.291]    [Pg.191]    [Pg.289]    [Pg.155]    [Pg.977]    [Pg.155]    [Pg.231]    [Pg.352]    [Pg.162]    [Pg.64]    [Pg.43]    [Pg.26]    [Pg.418]    [Pg.439]    [Pg.13]    [Pg.38]    [Pg.111]    [Pg.340]   
See also in sourсe #XX -- [ Pg.289 , Pg.289 , Pg.629 ]




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