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• W1980405919 abstract "Cytosolic sulfotransferase (SULT)-catalyzed sulfation regulates biological activities of various biosignaling molecules and metabolizes hydroxyl-containing drugs and xenobiotics. The universal sulfuryl group donor for SULT-catalyzed sulfation is adenosine 3′-phosphate 5′-phosphosulfate (PAPS), whereas the reaction products are a sulfated product and adenosine 3′,5′-diphosphate (PAP). Although SULT-catalyzed kinetic mechanisms have been studied since the 1980s, they remain unclear. Human SULT1A1 is an important phase II drug-metabolizing enzyme. Previously, isotope exchange at equilibrium indicated steady-state ordered mechanism with PAPS and PAP binding to the free SULT1A1 (Tyapochkin, E., Cook, P. F., and Chen, G. (2008) Biochemistry 47, 11894–11899). On the basis of activation of SULT1A1 by para-nitrophenyl sulfate (pNPS), an ordered bypass mechanism has been proposed where pNPS sulfates PAP prior to its release from the E·PAP complex regenerating E·PAPS. Data are consistent with uncompetitive substrate inhibition by naphthol as a result of formation of the E·PAP·naphthol dead-end complex; formation of the complex is corroborated by naphthol/PAP double inhibition experiments. pNPS activation data demonstrate an apparent ping-pong behavior with pNPS adding to E·PAP, and competitive inhibition by naphthol consistent with formation of the E·PAP·naphthol complex. Exchange against forward reaction flux (PAPS plus naphthol) beginning with [35S]PAPS and generating [35S]naphthyl sulfate is also consistent with pNPS intercepting the E·PAP complex. Overall, data are consistent with the proposed ordered bypass mechanism. Cytosolic sulfotransferase (SULT)-catalyzed sulfation regulates biological activities of various biosignaling molecules and metabolizes hydroxyl-containing drugs and xenobiotics. The universal sulfuryl group donor for SULT-catalyzed sulfation is adenosine 3′-phosphate 5′-phosphosulfate (PAPS), whereas the reaction products are a sulfated product and adenosine 3′,5′-diphosphate (PAP). Although SULT-catalyzed kinetic mechanisms have been studied since the 1980s, they remain unclear. Human SULT1A1 is an important phase II drug-metabolizing enzyme. Previously, isotope exchange at equilibrium indicated steady-state ordered mechanism with PAPS and PAP binding to the free SULT1A1 (Tyapochkin, E., Cook, P. F., and Chen, G. (2008) Biochemistry 47, 11894–11899). On the basis of activation of SULT1A1 by para-nitrophenyl sulfate (pNPS), an ordered bypass mechanism has been proposed where pNPS sulfates PAP prior to its release from the E·PAP complex regenerating E·PAPS. Data are consistent with uncompetitive substrate inhibition by naphthol as a result of formation of the E·PAP·naphthol dead-end complex; formation of the complex is corroborated by naphthol/PAP double inhibition experiments. pNPS activation data demonstrate an apparent ping-pong behavior with pNPS adding to E·PAP, and competitive inhibition by naphthol consistent with formation of the E·PAP·naphthol complex. Exchange against forward reaction flux (PAPS plus naphthol) beginning with [35S]PAPS and generating [35S]naphthyl sulfate is also consistent with pNPS intercepting the E·PAP complex. Overall, data are consistent with the proposed ordered bypass mechanism. Sulfotransferases (SULTs) 3The abbreviations used are: SULTsulfotransferaseSULT1A1simple phenol sulfotransferasePAPSadenosine 3′-phosphate 5′-phosphosulfatePAPadenosine 3′,5′-diphosphatepNPpara-nitrophenolpNPSpara-nitrophenyl sulfate. 3The abbreviations used are: SULTsulfotransferaseSULT1A1simple phenol sulfotransferasePAPSadenosine 3′-phosphate 5′-phosphosulfatePAPadenosine 3′,5′-diphosphatepNPpara-nitrophenolpNPSpara-nitrophenyl sulfate. are phase II drug-metabolizing enzymes that catalyze the sulfation (sulfonation) of various hydroxyl-containing compounds: biosignaling molecules such as hydroxysteroid hormones, thyroid hormones, glucocorticoid hormones, bile acids, neurotransmitters, and hydroxyl-containing xenobiotics (1Chapman E. Best M.D. Hanson S.R. Wong C.H. Angew. Chem. Int. Ed. Engl. 2004; 43: 3526-3548Crossref PubMed Scopus (234) Google Scholar, 2Coughtrie M.W. Pharmacogenomics J. 2002; 2: 297-308Crossref PubMed Scopus (183) Google Scholar, 3Duffel M.W. Marshal A.D. McPhie P. Sharma V. Jakoby W.B. Drug Metab. Rev. 2001; 33: 369-395Crossref PubMed Scopus (68) Google Scholar, 4Gamage N. Barnett A. Hempel N. Duggleby R.G. Windmill K.F. Martin J.L. McManus M.E. Toxicol. Sci. 2006; 90: 5-22Crossref PubMed Scopus (485) Google Scholar, 5Glatt H. Engelke C.E. Pabel U. Teubner W. Jones A.L. Coughtrie M.W. Andrae U. Falany C.N. Meinl W. Toxicol. Lett. 2000; 112–113: 341-348Crossref PubMed Scopus (119) Google Scholar, 6Pacifici G.M. Int. J. Clin. Pharmacol. Ther. 2004; 42: 488-495Crossref PubMed Scopus (50) Google Scholar, 7Runge-Morris M. Kocarek T.A. Curr. Drug Metab. 2005; 6: 299-307Crossref PubMed Scopus (65) Google Scholar, 8Wang L.Q. James M.O. Curr. Drug Metab. 2006; 7: 83-104Crossref PubMed Scopus (113) Google Scholar). The sulfation proceeds as shown in reaction 1, where the sulfuryl group donor is adenosine 3′-phosphate 5′-phosphosulfate (PAPS), and the reaction products are adenosine 3′,5′-diphosphate (PAP) and a sulfated product. R-OH+PAPS⇀↽SULTsR-OSO3H+PAPOne of the main biological functions of SULTs is the regulation of various hormones (9Falany C.N. FASEB J. 1997; 11: 206-216Crossref PubMed Scopus (517) Google Scholar). Sulfation of xenobiotics is mainly associated with detoxification, biotransformation of a relatively hydrophobic xenobiotic into a more water-soluble sulfuric ester that is readily excreted. However, in some cases sulfation can also cause bioactivation of procarcinogens and promutagens, leading to possible toxic effects (10Coughtrie M.W. Johnston L.E. Drug Metab. Dispos. 2001; 29: 522-528PubMed Google Scholar, 11Glatt H. Chem.-Biol. Interact. 2000; 129: 141-170Crossref PubMed Scopus (302) Google Scholar).Studies of the SULTs kinetic mechanisms began to appear in the early 1980s (12Duffel M.W. Jakoby W.B. J. Biol. Chem. 1981; 256: 11123-11127Abstract Full Text PDF PubMed Google Scholar). Although many SULT isoforms have been isolated and characterized, their biological functions and catalytic mechanisms are still not well understood. Human phenol sulfotransferase (SULT1A1) is one of the major detoxifying enzymes for phenolic xenobiotics; it also catalyzes the sulfation of endogenous hydroxyl biosignaling molecules. It has very broad substrate specificity and high activity toward most phenolic compounds. SULT1A1 is also widely distributed in the human body. On the basis of isotope exchange at equilibrium, we showed that the kinetic mechanism for human SULT1A1 is steady-state-ordered with PAPS binding to the protein first, and PAP released last (13Tyapochkin E. Cook P.F. Chen G. Biochemistry. 2008; 47: 11894-11899Crossref PubMed Scopus (17) Google Scholar).Substrate inhibition by the hydroxyl substrate (sulfate acceptor) is a common feature of most cytosolic SULTs (14Barnett A.C. Tsvetanov S. Gamage N. Martin J.L. Duggleby R.G. McManus M.E. J. Biol. Chem. 2004; 279: 18799-18805Abstract Full Text Full Text PDF PubMed Scopus (47) Google Scholar, 15Miksits M. Maier-Salamon A. Aust S. Thalhammer T. Reznicek G. Kunert O. Haslinger E. Szekeres T. Jaeger W. Xenobiotica. 2005; 35: 1101-1119Crossref PubMed Scopus (80) Google Scholar). Inhibition of SULT1A1 has been observed by the substrate, naphthol. There are a number of different mechanisms that have been proposed for substrate inhibition, but the mechanism remains unclear. A ternary complex formed between substrate and the enzyme·PAP complex is the most likely possibility in an ordered mechanism, but binding to free enzyme is also possible (12Duffel M.W. Jakoby W.B. J. Biol. Chem. 1981; 256: 11123-11127Abstract Full Text PDF PubMed Google Scholar, 16Beckmann J.D. Burkett R.J. Sharpe M. Giannunzio L. Johnston D. Abbey S. Wyman A. Sung L. Biochim. Biophys. Acta. 2003; 1648: 134-139Crossref PubMed Scopus (9) Google Scholar). It is also possible, but unlikely, that substrate could bind to central complexes. In addition, binding of two substrate molecules to the active site has been proposed (4Gamage N. Barnett A. Hempel N. Duggleby R.G. Windmill K.F. Martin J.L. McManus M.E. Toxicol. Sci. 2006; 90: 5-22Crossref PubMed Scopus (485) Google Scholar, 14Barnett A.C. Tsvetanov S. Gamage N. Martin J.L. Duggleby R.G. McManus M.E. J. Biol. Chem. 2004; 279: 18799-18805Abstract Full Text Full Text PDF PubMed Scopus (47) Google Scholar). A SULT1A1 crystal structure was solved that showed two molecules of p-nitrophenol (pNP) in the same active site. However, computer modeling of this structure indicated that the active site could not easily accommodate even one molecule of a larger substrate such as β-estradiol (17Gamage N.U. Duggleby R.G. Barnett A.C. Tresillian M. Latham C.F. Liyou N.E. McManus M.E. Martin J.L. J. Biol. Chem. 2003; 278: 7655-7662Abstract Full Text Full Text PDF PubMed Scopus (139) Google Scholar). Other SULT crystal structures solved with the bound substrate indicated that only one substrate is possible in the crystal structure (18Kakuta Y. Pedersen L.G. Carter C.W. Negishi M. Pedersen L.C. Nat. Struct. Biol. 1997; 4: 904-908Crossref PubMed Scopus (230) Google Scholar, 19Pakhomova S. Buck J. Newcomer M.E. Protein Sci. 2005; 14: 176-182Crossref PubMed Scopus (9) Google Scholar, 20Pakhomova S. Kobayashi M. Buck J. Newcomer M.E. Nat. Struct. Biol. 2001; 8: 447-451Crossref PubMed Scopus (29) Google Scholar, 21Pakhomova S. Luz J.G. Kobayashi M. Mellman D. Buck J. Newcomer M.E. Acta Crystallogr. D Biol. Crystallogr. 2000; 56: 1641-1643Crossref PubMed Scopus (9) Google Scholar, 22Rehse P.H. Zhou M. Lin S.X. Biochem. J. 2002; 364: 165-171Crossref PubMed Scopus (69) Google Scholar, 23Shevtsov S. Petrotchenko E.V. Pedersen L.C. Negishi M. Environ. Health Perspect. 2003; 111: 884-888Crossref PubMed Scopus (56) Google Scholar).para-Nitrophenyl sulfate (pNPS) has been used for phenol SULTs enzyme activity assays (24Frame L.T. Ozawa S. Nowell S.A. Chou H.C. DeLongchamp R.R. Doerge D.R. Lang N.P. Kadlubar F.F. Drug Metab. Dispos. 2000; 28: 1063-1068PubMed Google Scholar, 25Chen G. Battaglia E. Senay C. Falany C.N. Radominska-Pandya A. Protein Sci. 1999; 8: 2151-2157Crossref PubMed Scopus (29) Google Scholar, 26Chen G. Rabjohn P.A. York J.L. Wooldridge C. Zhang D. Falany C.N. Radominska-Pandya A. Biochemistry. 2000; 39: 16000-16007Crossref PubMed Scopus (28) Google Scholar, 27Lin E.S. Yang Y.S. Anal. Biochem. 1998; 264: 111-117Crossref PubMed Scopus (21) Google Scholar). Recently, we have been interested in the mechanisms for pNPS activation of SULT1A1-catalyzed sulfation of other phenol substrates, such as naphthols. On the basis of this activation by pNPS, a mechanism was proposed that requires sulfation of PAP prior to its release, from the E·PAP complex (Scheme 1), i.e. pNPS binds to E·PAP and generates the E·PAPS·pNP complex, which dissociates pNP and generates the E·PAPS complex.In this work, the proposed mechanism was tested using the double inhibition method of Yonetani and Theorell (28Yonetani T. Theorell H. Arch. Biochem. Biophys. 1964; 106: 243-251Crossref PubMed Scopus (216) Google Scholar), which provides information on whether binding of two inhibitors is mutually exclusive. Double inhibition experiments have been successful in demonstrating whether the binding of two inhibitors is mutually exclusive, or whether they show interference or synergism in binding (28Yonetani T. Theorell H. Arch. Biochem. Biophys. 1964; 106: 243-251Crossref PubMed Scopus (216) Google Scholar, 29Cook P.F. Cleland W.W. Enzyme Kinetics and Mechanism. Garland Science, London2007: 191-195Google Scholar, 30Kiick D.M. Harris B.G. Cook P.F. Biochemistry. 1986; 25: 227-236Crossref PubMed Scopus (44) Google Scholar, 31Leskovac V. Comprehensive Enzyme Kinetics. Springer, New York2003: 91-93Google Scholar, 32Northrop D.B. Cleland W.W. J. Biol. Chem. 1974; 249: 2928-2931Abstract Full Text PDF PubMed Google Scholar). In addition, substrate inhibition by the hydroxyl substrate and exchange against forward reaction flux were used as probes of the mechanism. Data are discussed in terms of the overall mechanism of SULT1A1. Sulfotransferases (SULTs) 3The abbreviations used are: SULTsulfotransferaseSULT1A1simple phenol sulfotransferasePAPSadenosine 3′-phosphate 5′-phosphosulfatePAPadenosine 3′,5′-diphosphatepNPpara-nitrophenolpNPSpara-nitrophenyl sulfate. 3The abbreviations used are: SULTsulfotransferaseSULT1A1simple phenol sulfotransferasePAPSadenosine 3′-phosphate 5′-phosphosulfatePAPadenosine 3′,5′-diphosphatepNPpara-nitrophenolpNPSpara-nitrophenyl sulfate. are phase II drug-metabolizing enzymes that catalyze the sulfation (sulfonation) of various hydroxyl-containing compounds: biosignaling molecules such as hydroxysteroid hormones, thyroid hormones, glucocorticoid hormones, bile acids, neurotransmitters, and hydroxyl-containing xenobiotics (1Chapman E. Best M.D. Hanson S.R. Wong C.H. Angew. Chem. Int. Ed. Engl. 2004; 43: 3526-3548Crossref PubMed Scopus (234) Google Scholar, 2Coughtrie M.W. Pharmacogenomics J. 2002; 2: 297-308Crossref PubMed Scopus (183) Google Scholar, 3Duffel M.W. Marshal A.D. McPhie P. Sharma V. Jakoby W.B. Drug Metab. Rev. 2001; 33: 369-395Crossref PubMed Scopus (68) Google Scholar, 4Gamage N. Barnett A. Hempel N. Duggleby R.G. Windmill K.F. Martin J.L. McManus M.E. Toxicol. Sci. 2006; 90: 5-22Crossref PubMed Scopus (485) Google Scholar, 5Glatt H. Engelke C.E. Pabel U. Teubner W. Jones A.L. Coughtrie M.W. Andrae U. Falany C.N. Meinl W. Toxicol. Lett. 2000; 112–113: 341-348Crossref PubMed Scopus (119) Google Scholar, 6Pacifici G.M. Int. J. Clin. Pharmacol. Ther. 2004; 42: 488-495Crossref PubMed Scopus (50) Google Scholar, 7Runge-Morris M. Kocarek T.A. Curr. Drug Metab. 2005; 6: 299-307Crossref PubMed Scopus (65) Google Scholar, 8Wang L.Q. James M.O. Curr. Drug Metab. 2006; 7: 83-104Crossref PubMed Scopus (113) Google Scholar). The sulfation proceeds as shown in reaction 1, where the sulfuryl group donor is adenosine 3′-phosphate 5′-phosphosulfate (PAPS), and the reaction products are adenosine 3′,5′-diphosphate (PAP) and a sulfated product. R-OH+PAPS⇀↽SULTsR-OSO3H+PAP sulfotransferase simple phenol sulfotransferase adenosine 3′-phosphate 5′-phosphosulfate adenosine 3′,5′-diphosphate para-nitrophenol para-nitrophenyl sulfate. sulfotransferase simple phenol sulfotransferase adenosine 3′-phosphate 5′-phosphosulfate adenosine 3′,5′-diphosphate para-nitrophenol para-nitrophenyl sulfate. One of the main biological functions of SULTs is the regulation of various hormones (9Falany C.N. FASEB J. 1997; 11: 206-216Crossref PubMed Scopus (517) Google Scholar). Sulfation of xenobiotics is mainly associated with detoxification, biotransformation of a relatively hydrophobic xenobiotic into a more water-soluble sulfuric ester that is readily excreted. However, in some cases sulfation can also cause bioactivation of procarcinogens and promutagens, leading to possible toxic effects (10Coughtrie M.W. Johnston L.E. Drug Metab. Dispos. 2001; 29: 522-528PubMed Google Scholar, 11Glatt H. Chem.-Biol. Interact. 2000; 129: 141-170Crossref PubMed Scopus (302) Google Scholar). Studies of the SULTs kinetic mechanisms began to appear in the early 1980s (12Duffel M.W. Jakoby W.B. J. Biol. Chem. 1981; 256: 11123-11127Abstract Full Text PDF PubMed Google Scholar). Although many SULT isoforms have been isolated and characterized, their biological functions and catalytic mechanisms are still not well understood. Human phenol sulfotransferase (SULT1A1) is one of the major detoxifying enzymes for phenolic xenobiotics; it also catalyzes the sulfation of endogenous hydroxyl biosignaling molecules. It has very broad substrate specificity and high activity toward most phenolic compounds. SULT1A1 is also widely distributed in the human body. On the basis of isotope exchange at equilibrium, we showed that the kinetic mechanism for human SULT1A1 is steady-state-ordered with PAPS binding to the protein first, and PAP released last (13Tyapochkin E. Cook P.F. Chen G. Biochemistry. 2008; 47: 11894-11899Crossref PubMed Scopus (17) Google Scholar). Substrate inhibition by the hydroxyl substrate (sulfate acceptor) is a common feature of most cytosolic SULTs (14Barnett A.C. Tsvetanov S. Gamage N. Martin J.L. Duggleby R.G. McManus M.E. J. Biol. Chem. 2004; 279: 18799-18805Abstract Full Text Full Text PDF PubMed Scopus (47) Google Scholar, 15Miksits M. Maier-Salamon A. Aust S. Thalhammer T. Reznicek G. Kunert O. Haslinger E. Szekeres T. Jaeger W. Xenobiotica. 2005; 35: 1101-1119Crossref PubMed Scopus (80) Google Scholar). Inhibition of SULT1A1 has been observed by the substrate, naphthol. There are a number of different mechanisms that have been proposed for substrate inhibition, but the mechanism remains unclear. A ternary complex formed between substrate and the enzyme·PAP complex is the most likely possibility in an ordered mechanism, but binding to free enzyme is also possible (12Duffel M.W. Jakoby W.B. J. Biol. Chem. 1981; 256: 11123-11127Abstract Full Text PDF PubMed Google Scholar, 16Beckmann J.D. Burkett R.J. Sharpe M. Giannunzio L. Johnston D. Abbey S. Wyman A. Sung L. Biochim. Biophys. Acta. 2003; 1648: 134-139Crossref PubMed Scopus (9) Google Scholar). It is also possible, but unlikely, that substrate could bind to central complexes. In addition, binding of two substrate molecules to the active site has been proposed (4Gamage N. Barnett A. Hempel N. Duggleby R.G. Windmill K.F. Martin J.L. McManus M.E. Toxicol. Sci. 2006; 90: 5-22Crossref PubMed Scopus (485) Google Scholar, 14Barnett A.C. Tsvetanov S. Gamage N. Martin J.L. Duggleby R.G. McManus M.E. J. Biol. Chem. 2004; 279: 18799-18805Abstract Full Text Full Text PDF PubMed Scopus (47) Google Scholar). A SULT1A1 crystal structure was solved that showed two molecules of p-nitrophenol (pNP) in the same active site. However, computer modeling of this structure indicated that the active site could not easily accommodate even one molecule of a larger substrate such as β-estradiol (17Gamage N.U. Duggleby R.G. Barnett A.C. Tresillian M. Latham C.F. Liyou N.E. McManus M.E. Martin J.L. J. Biol. Chem. 2003; 278: 7655-7662Abstract Full Text Full Text PDF PubMed Scopus (139) Google Scholar). Other SULT crystal structures solved with the bound substrate indicated that only one substrate is possible in the crystal structure (18Kakuta Y. Pedersen L.G. Carter C.W. Negishi M. Pedersen L.C. Nat. Struct. Biol. 1997; 4: 904-908Crossref PubMed Scopus (230) Google Scholar, 19Pakhomova S. Buck J. Newcomer M.E. Protein Sci. 2005; 14: 176-182Crossref PubMed Scopus (9) Google Scholar, 20Pakhomova S. Kobayashi M. Buck J. Newcomer M.E. Nat. Struct. Biol. 2001; 8: 447-451Crossref PubMed Scopus (29) Google Scholar, 21Pakhomova S. Luz J.G. Kobayashi M. Mellman D. Buck J. Newcomer M.E. Acta Crystallogr. D Biol. Crystallogr. 2000; 56: 1641-1643Crossref PubMed Scopus (9) Google Scholar, 22Rehse P.H. Zhou M. Lin S.X. Biochem. J. 2002; 364: 165-171Crossref PubMed Scopus (69) Google Scholar, 23Shevtsov S. Petrotchenko E.V. Pedersen L.C. Negishi M. Environ. Health Perspect. 2003; 111: 884-888Crossref PubMed Scopus (56) Google Scholar). para-Nitrophenyl sulfate (pNPS) has been used for phenol SULTs enzyme activity assays (24Frame L.T. Ozawa S. Nowell S.A. Chou H.C. DeLongchamp R.R. Doerge D.R. Lang N.P. Kadlubar F.F. Drug Metab. Dispos. 2000; 28: 1063-1068PubMed Google Scholar, 25Chen G. Battaglia E. Senay C. Falany C.N. Radominska-Pandya A. Protein Sci. 1999; 8: 2151-2157Crossref PubMed Scopus (29) Google Scholar, 26Chen G. Rabjohn P.A. York J.L. Wooldridge C. Zhang D. Falany C.N. Radominska-Pandya A. Biochemistry. 2000; 39: 16000-16007Crossref PubMed Scopus (28) Google Scholar, 27Lin E.S. Yang Y.S. Anal. Biochem. 1998; 264: 111-117Crossref PubMed Scopus (21) Google Scholar). Recently, we have been interested in the mechanisms for pNPS activation of SULT1A1-catalyzed sulfation of other phenol substrates, such as naphthols. On the basis of this activation by pNPS, a mechanism was proposed that requires sulfation of PAP prior to its release, from the E·PAP complex (Scheme 1), i.e. pNPS binds to E·PAP and generates the E·PAPS·pNP complex, which dissociates pNP and generates the E·PAPS complex. In this work, the proposed mechanism was tested using the double inhibition method of Yonetani and Theorell (28Yonetani T. Theorell H. Arch. Biochem. Biophys. 1964; 106: 243-251Crossref PubMed Scopus (216) Google Scholar), which provides information on whether binding of two inhibitors is mutually exclusive. Double inhibition experiments have been successful in demonstrating whether the binding of two inhibitors is mutually exclusive, or whether they show interference or synergism in binding (28Yonetani T. Theorell H. Arch. Biochem. Biophys. 1964; 106: 243-251Crossref PubMed Scopus (216) Google Scholar, 29Cook P.F. Cleland W.W. Enzyme Kinetics and Mechanism. Garland Science, London2007: 191-195Google Scholar, 30Kiick D.M. Harris B.G. Cook P.F. Biochemistry. 1986; 25: 227-236Crossref PubMed Scopus (44) Google Scholar, 31Leskovac V. Comprehensive Enzyme Kinetics. Springer, New York2003: 91-93Google Scholar, 32Northrop D.B. Cleland W.W. J. Biol. Chem. 1974; 249: 2928-2931Abstract Full Text PDF PubMed Google Scholar). In addition, substrate inhibition by the hydroxyl substrate and exchange against forward reaction flux were used as probes of the mechanism. Data are discussed in terms of the overall mechanism of SULT1A1." @default.
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• W1980405919 title "para-Nitrophenyl Sulfate Activation of Human Sulfotransferase 1A1 Is Consistent with Intercepting the E·PAP Complex and Reformation of E·PAPS" @default.
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