Adenosine-S -phosphosulfate

NMR, nuclear magnetic resonance mV, millivolt pCMB, p hloromercuribenzoate pCMS, p-chloromercuriphenyl sulfonate PMS, phenazine methosulfate EDTA, ethylenediaminetetraacetate SDS, sodium dodecyl sulfate TTFA, 2-thenoyltriflu-oroacetone ETP, submitochondrial (electron transfer) particles MVH, reduced methyl viologen DEAE-cellulose, diethylaminoethyl cellulose succ, succinate APS, adenosine S -phosphosulfate PAPS, 3 -phosphoadenosine 5 -phosphosulfate. Other abbreviations are standard [see JBC 244, 2 (1969)]. 

Adenosine 3 -monophosphate, trans-hydrogenase and, 71 Adenosine 3, 5-monophosphate, trans-hydrogenase and, 71 Adenosine S -phosphosulfate, formation of, 279... 

Sulfate activation formation of the active sulfates, Phosphoadenosinephosphosulhite (see), (PAK) and adenosine S -phosphosulfate (APS). PAPS is the substrate of sulfotransferases in the synthesis of sulfate esters. APS is the substrate of sulfate assimilation and sulfate respiration. 

Fig. 3. Regulation of the bound pathway for the assimilation of sulfate into cysteine and associated processes. Carrier refers to an endogenous thiol of uncertain identity in higher plants. Enzymes associated with the sulfate assimilation pathway and the synthesis of O-acetylseiine are (1) high-ailinity sulfate uptake mechanism, (2) ATP-sulfurylase, (3) adenosine S -phosphosulfate (APS) sulfotransferase, (4) organic thiosulfate reductase, (5) cysteine synthase, and (6) serine transacetylase. Cysteine sulfhydrase (7), an enzyme of cysteine catabolism, and nitrate reductase (8), the first enzyme of the nitrate assimilation pathway, are also shown. Inhibitory control of the pathways is shown by discontinuous lines (----) and enhancement by continuous lines (------).

Some alcohols, arylamines, and phenols are sulfated. The sulfate donor in these and other biologic sulfation reactions (eg, sulfation of steroids, glycosaminoglycans, glycolipids, and glycoproteins) is adenosine 3 -phos-phate-S -phosphosulfate (PAPS) (Chapter 24) this compound is called active sulfate. ... 

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. 

Fukui, S., Yoshida, H., and Yamashina, I. Sulfohydrolytic degradation of 3 -phosphoadenosine 5 -phosphosulfate and adenosine 5 -phosphosulfate by enzymes of a nucleotide pyrophosphatase nature. J. Biochem. (Tokyo) 90, 1537-1540 (1981). 

Roger, K. M., White, G. F., and Dodgson, K. S., Purification and properties of bovine fiver lysosomal adenosine 5 -phosphosulfate sulfohydrolase. Biochim. Biophys. Acta 527, 70-85... 

Non-carbon-bonded sulfur compounds. These are primarily ester sulfates (-C-0-S, sulfur bonded to oxygen) such as phenolic sulfates, sulfamic acid (-C-N-S), sulfated polysaccharides, and adenosine-5 -phosphosulfate (APS). Approximately half of the total sulfur in soil organic matter is present in this form. 

RapidChek II SRB Test Kit is manufactured by Strategic Diagnostics, Inc. (U.S.). This test kit detects the presence of SRB in water bottom samples in less than twenty minutes. Antibodies are used to detect the enzyme adenosine-5 -phosphosulfate (APS) reductase, which is produced by all strains of SRB. 

Adeno8ine-3 -phosphate-5 phosphosulfate (PAPS) Adenosine-S -phospho-selenate... 

The activation mechanism of phosphosulfate linkages (P—O —S)has been studied to understand the chemistry of biological sulfate-transfer reactions of phosphosul-fates of adenosine (APS and PAPS). Several phosphosul-fates were prepared and subjected to several nucleophilic reactions including hydrolysis. In general, phosphosulfates are stable in neutral aqueous mediay but become labile under acidic conditions, resulting in selective S—O fission. This S—O fission appears to occur by unimolecular elimination of sulfur trioxide, which can react with a nucleophilic acceptor, leading to a sulfate-transfer reaction. This process can be accelerated by Mg2+ ion when the solvent is of low water content. Under neutral conditions, divalent metal ions also were found to catalyze nucleophilic reactions, but these occurred on phosphorus to result in exclusive P-O fission. 

The biochemical pathway of both assimilatory and dissimilatory sulfate reduction is illustrated in Figure 1. The details of the dissimilatory reduction pathway are useful for understanding the origin of bacterial stable isotopic fractionations. The overall pathways require the transfer of eight electrons, and proceed through a number of intermediate steps. The reduction of sulfate requires activation by ATP (adenosine triphosphate) to form adenosine phosphosulfate (APS). The enzyme ATP sulfurylase catalyzes this reaction. In dissimilatory reduction, the sulfate moiety of APS is reduced to sulfite (SO3 ) by the enzyme APS reductase, whereas in assimilatory reduction APS is further phosphorylated to phospho-adenosine phosphosulfate (PAPS) before reduction to the oxidation state of sulfite and sulfide. Although the reduction reactions occur in the cell s cytoplasm (i.e., the sulfate enters the cell), the electron transport chain for dissimilatory sulfate reduction occurs in proteins that are peiiplasmic (within the bacterial cell wall). The enzyme hydrogenase... 

Conjugation reactions in which electrophilic adenosine-containing cofactors such as ATP, phosphoadenosine phosphosulfate (PAPS), acet-ylcoenzyme A (acetylCoA), uridine diphosphate glucuronic acid (UDPGA), or S-adenosylmethio-nine (SAM) react with nucleophilic groups such as -OH or -NHg... 

Sulfate reduction reduction of the sulfote ion S04 " to the sulfide ion S, in which the hexavalent, positive sulfur of the sulfate is converted to the divalent, negative form. S.r. must be preceded by Sulfate activation (see). The substrate of enzymatic S.r. is therefore either adenosine phosphosulfate (APS) or phosphoadenosinephosphosulfate (PAPS). The enzy-mology of S.r. has been studied in particular in enzyme preparations from baker s yeast (Saccharomy-ces cerevisiae) and the anaerobic bacterium Desulfo-vibrio desulfuricans. The former organism performs assimilatory S.r. (see Sulfate assimilation), Ae latter dissimilatory S.r. (see Sulfate respiration). 

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. 

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