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Gene Review

SULT1A3  -  sulfotransferase family, cytosolic, 1A,...

Homo sapiens

Synonyms: HAST, HAST3, M-PST, ST1A3, ST1A3/ST1A4, ...
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Disease relevance of SULT1A3


Psychiatry related information on SULT1A3

  • The contrasting patterns of sparing and loss of STM and LTM in PD and global amnesia were present for both recognition and recall [5].
  • The traditional concept of memory disorder is deficiency of the long-term (LTM) but not short-term (STM) component of memory [5].
  • Ninety patients with a previous subarachnoid haemorrhage (SAH) were given a set of memory tests comprising immediate free recall of words (indexing long-term memory, LTM, and short-term memory, STM), final free recall of words (indexing LTM), final cued recall of words (indexing LTM), and a digit span test (indexing working memory, WM) [6].
  • It is argued that the results are more consistent with psycholinguistic models than nonlinguistic models of STM, and implications for current STM models are discussed [7].

High impact information on SULT1A3


Chemical compound and disease context of SULT1A3

  • Isolation of Salmonella enterica subspecies enterica serovar Paratyphi B dT+, or Salmonella Java, from Indonesia and alteration of the d-tartrate fermentation phenotype by disrupting the ORF STM 3356 [11].
  • Trimeric Achromobacter cycloclastes Cu-containing nitrite reductase (CuNIR) proteins adsorbed on gold and graphite have been studied by ambient STM and in situ AFM [12].
  • Some excellent results which might indicate clinically unknown effects of toluene such as hearing loss, impairments of time discrimination, and improvements of STM were also demonstrated [13].

Biological context of SULT1A3


Anatomical context of SULT1A3

  • Pharmacogenetic studies of TS and TL PST activities in the human blood platelet showed that the activities of these two isoforms were regulated by separate genetic polymorphisms [16].
  • We recently cloned a cDNA for human liver TL PST and expressed it in COS-1 cells [17].
  • DNA from NIGMS Human/Rodent Somatic Cell Hybrid Mapping Panels 1 and 2 was screened by use of the PCR, and the STM gene was mapped to chromosome 16 [17].
  • As a first step toward cloning a cDNA for TL PST, the enzyme was purified from jejunal mucosa, the human tissue with the highest known specific activity, and purified TL PST was subjected to limited proteolysis and amino acid sequencing [18].
  • The inhibition profiles of the 3,3'-T2 sulfotransferase activities of liver and kidney cytosol obtained by addition of 10 micromol/L of the various analogs were better correlated with the inhibition profile of SULT1A1 than with that of SULT1A3 [19].

Associations of SULT1A3 with chemical compounds

  • Further studies using point-mutated SULT1A3s mutated at amino acid residues in these two regions and deletional mutants missing residues 84-86 and 84-90 implicate residue Glu-146 (in variable Region II of SULT1A3), as well as the presence of residues 84-90 of variable Region I, in the stereospecificity in the absence of Mn(2+) [10].
  • Structure-function relationships in the stereospecific and manganese-dependent 3,4-dihydroxyphenylalanine/tyrosine-sulfating activity of human monoamine-form phenol sulfotransferase, SULT1A3 [10].
  • T1AM, the most active thyronamine pharmacologically, was associated with the greatest SULT activity of the thyronamines tested in the liver pool and in both the expressed SULT1A3 and SULT1E1 preparations [20].
  • Moreover, when estrone (which selectively inhibits expressed SULT1E1 and SULT1A3) was included in intestinal incubations, the high-affinity component of the Eadie-Hofstee plot for EE sulfation was inhibited, converting the plot from biphasic to monophasic [21].
  • If the expression levels in tissues are additionally taken into account, SULT1A3 might be the predominant form for the sulphonation of ethanol in vivo, although a robust estimate requires further studies [22].

Physical interactions of SULT1A3


Enzymatic interactions of SULT1A3


Regulatory relationships of SULT1A3

  • The ability of hM-PST to sulfate a number of xenobiotics was examined and compared with the bacterially expressed human phenol-sulfating form of PST (hP-PST) [3].

Other interactions of SULT1A3

  • The change of a single amino acid, E146A, was sufficient to transform the catalytic properties and substrate preference of SULT1A3, such that they closely resembled those of SULT1A1 [14].
  • In humans, catecholamines such as dopamine are extensively sulfated, and a SULT isoform (SULT1A3 or the monoamine-sulfating form of phenolsulfotransferase) has evolved with considerable selectivity for dopamine and other biogenic amines [14].
  • The remaining enzymes studied (SULT1A3, 1C1, 1E1, 2A1, 2B1a, 2B1b, 4A1 and NAT1) did not indicate any activation of N-OH-MeAalphaC [25].
  • From these data, we conclude that human liver TS-PST but not TL-PST or DHEA-ST can metabolically activate the proximate human carcinogen N-OH-ABP to a reactive sulfuric acid ester intermediate that binds covalently to DNA [26].
  • We previously cloned and expressed a cDNA for human liver TL PST and localized its gene, STM, to human chromosome 16p11.2, a region of the chromosome to which the Batten disease gene is also localized [27].

Analytical, diagnostic and therapeutic context of SULT1A3


  1. Thermostable (SULT1A1) and thermolabile (SULT1A3) phenol sulfotransferases in human osteosarcoma and osteoblast cells. Dubin, R.L., Hall, C.M., Pileri, C.L., Kudlacek, P.E., Li, X.Y., Yee, J.A., Johnson, M.L., Anderson, R.J. Bone (2001) [Pubmed]
  2. Generation and release of nitrotyrosine O-sulfate by HepG2 human hepatoma cells upon SIN-1 stimulation: identification of SULT1A3 as the enzyme responsible. Yasuda, S., Idell, S., Liu, M.C. Biochem. J. (2007) [Pubmed]
  3. Bacterial expression and kinetic characterization of the human monoamine-sulfating form of phenol sulfotransferase. Ganguly, T.C., Krasnykh, V., Falany, C.N. Drug Metab. Dispos. (1995) [Pubmed]
  4. Expression of human estrogen sulfotransferase in Salmonella typhimurium: differences between hHST and hEST in the enantioselective activation of 1-hydroxyethylpyrene to a mutagen. Hagen, M., Pabel, U., Landsiedel, R., Bartsch, I., Falany, C.N., Glatt, H. Chem. Biol. Interact. (1998) [Pubmed]
  5. Double dissociation of short-term and long-term memory for nonverbal material in Parkinson's disease and global amnesia. A further analysis. Sullivan, E.V., Sagar, H.J. Brain (1991) [Pubmed]
  6. Subarachnoid blood on CT and memory dysfunctions in aneurysmal subarachnoid hemorrhage. Larsson, C., Forssell, A., Rönnberg, J., Lindberg, M., Nilsson, L.G., Fodstad, H. Acta neurologica Scandinavica. (1994) [Pubmed]
  7. The phonological similarity effect in serial recognition. Nimmo, L.M., Roodenrys, S. Memory (Hove, England) (2005) [Pubmed]
  8. Catecholamine metabolic pathways and exercise training. Plasma and urine catecholamines, metabolic enzymes, and chromogranin-A. Rogers, P.J., Tyce, G.M., Weinshilboum, R.M., O'Connor, D.T., Bailey, K.R., Bove, A.A. Circulation (1991) [Pubmed]
  9. Active site mutations and substrate inhibition in human sulfotransferase 1A1 and 1A3. Barnett, A.C., Tsvetanov, S., Gamage, N., Martin, J.L., Duggleby, R.G., McManus, M.E. J. Biol. Chem. (2004) [Pubmed]
  10. Structure-function relationships in the stereospecific and manganese-dependent 3,4-dihydroxyphenylalanine/tyrosine-sulfating activity of human monoamine-form phenol sulfotransferase, SULT1A3. Pai, T.G., Oxendine, I., Sugahara, T., Suiko, M., Sakakibara, Y., Liu, M.C. J. Biol. Chem. (2003) [Pubmed]
  11. Isolation of Salmonella enterica subspecies enterica serovar Paratyphi B dT+, or Salmonella Java, from Indonesia and alteration of the d-tartrate fermentation phenotype by disrupting the ORF STM 3356. Han, K.H., Choi, S.Y., Lee, J.H., Lee, H., Shin, E.H., Agtini, M.D., von Seidlein, L., Ochiai, R.L., Clemens, J.D., Wain, J., Hahn, J.S., Lee, B.K., Song, M., Chun, J., Kim, D.W. J. Med. Microbiol. (2006) [Pubmed]
  12. Ambient STM and in situ AFM study of nitrite reductase proteins adsorbed on gold and graphite: influence of the substrate on protein interactions. Contera, S.A., Iwasaki, H., Suzuki, S. Ultramicroscopy. (2003) [Pubmed]
  13. Behavioral approaches to toluene intoxication. Saito, K., Wada, H. Environmental research. (1993) [Pubmed]
  14. A single amino acid, glu146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3. Dajani, R., Hood, A.M., Coughtrie, M.W. Mol. Pharmacol. (1998) [Pubmed]
  15. Human SULT1A3 pharmacogenetics: gene duplication and functional genomic studies. Hildebrandt, M.A., Salavaggione, O.E., Martin, Y.N., Flynn, H.C., Jalal, S., Wieben, E.D., Weinshilboum, R.M. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  16. Human phenol sulfotransferase pharmacogenetics: STP1 gene cloning and structural characterization. Raftogianis, R.B., Her, C., Weinshilboum, R.M. Pharmacogenetics (1996) [Pubmed]
  17. Thermolabile phenol sulfotransferase gene (STM): localization to human chromosome 16p11.2. Aksoy, I.A., Callen, D.F., Apostolou, S., Her, C., Weinshilboum, R.M. Genomics (1994) [Pubmed]
  18. Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization. Wood, T.C., Aksoy, I.A., Aksoy, S., Weinshilboum, R.M. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  19. Characterization of human iodothyronine sulfotransferases. Kester, M.H., Kaptein, E., Roest, T.J., van Dijk, C.H., Tibboel, D., Meinl, W., Glatt, H., Coughtrie, M.W., Visser, T.J. J. Clin. Endocrinol. Metab. (1999) [Pubmed]
  20. Thyronamines are substrates for human liver sulfotransferases. Pietsch, C.A., Scanlan, T.S., Anderson, R.J. Endocrinology (2007) [Pubmed]
  21. Sulfotransferase 1E1 is a low km isoform mediating the 3-O-sulfation of ethinyl estradiol. Schrag, M.L., Cui, D., Rushmore, T.H., Shou, M., Ma, B., Rodrigues, A.D. Drug Metab. Dispos. (2004) [Pubmed]
  22. Sulpho-conjugation of ethanol in humans in vivo and by individual sulphotransferase forms in vitro. Schneider, H., Glatt, H. Biochem. J. (2004) [Pubmed]
  23. Crystal structure of human catecholamine sulfotransferase. Bidwell, L.M., McManus, M.E., Gaedigk, A., Kakuta, Y., Negishi, M., Pedersen, L., Martin, J.L. J. Mol. Biol. (1999) [Pubmed]
  24. Human phenol sulfotransferase: correlation of brain and platelet activities. Young, W.F., Laws, E.R., Sharbrough, F.W., Weinshilboum, R.M. J. Neurochem. (1985) [Pubmed]
  25. Bioactivation of the heterocyclic aromatic amine 2-amino-3-methyl-9H-pyrido [2,3-b]indole (MeAalphaC) in recombinant test systems expressing human xenobiotic-metabolizing enzymes. Glatt, H., Pabel, U., Meinl, W., Frederiksen, H., Frandsen, H., Muckel, E. Carcinogenesis (2004) [Pubmed]
  26. Metabolic activation of the N-hydroxy derivative of the carcinogen 4-aminobiphenyl by human tissue sulfotransferases. Chou, H.C., Lang, N.P., Kadlubar, F.F. Carcinogenesis (1995) [Pubmed]
  27. Human thermolabile phenol sulfotransferase gene (STM): molecular cloning and structural characterization. Aksoy, I.A., Weinshilboum, R.M. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  28. 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. Dajani, R., Cleasby, A., Neu, M., Wonacott, A.J., Jhoti, H., Hood, A.M., Modi, S., Hersey, A., Taskinen, J., Cooke, R.M., Manchee, G.R., Coughtrie, M.W. J. Biol. Chem. (1999) [Pubmed]
  29. N-Acetyltransferases, sulfotransferases and heterocyclic amine activation in the breast. Williams, J.A., Stone, E.M., Fakis, G., Johnson, N., Cordell, J.A., Meinl, W., Glatt, H., Sim, E., Phillips, D.H. Pharmacogenetics (2001) [Pubmed]
  30. Sulfation of thyroid hormone and dopamine during human development: ontogeny of phenol sulfotransferases and arylsulfatase in liver, lung, and brain. Richard, K., Hume, R., Kaptein, E., Stanley, E.L., Visser, T.J., Coughtrie, M.W. J. Clin. Endocrinol. Metab. (2001) [Pubmed]
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