Sulfotransferase

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<StructureSection load='' size='350' side='right' scene='49/491888/Cv/2' caption='Human estrogen sulfotransferase dimer complex with cofactor PAP, [[1hy3]]'>
<StructureSection load='' size='350' side='right' scene='49/491888/Cv/2' caption='Human estrogen sulfotransferase dimer complex with cofactor PAP, [[1hy3]]'>
== Function ==
== Function ==
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'''Sulfotransferase''' (ST) are enzymes which catalyze the transfer of a sulfate group from a donor molecule to an acceptor alcohol or amine. The acceptors are hormones, neurotransmitters, drugs and xenobiotic compounds. The addition of a charged chemical moiety to the above carbon-rich water-insoluble molecules, make them more soluble and thus transportable in the circulatory system<ref>PMID:20136513</ref>. The various human STs are named SULT1, SULT2, SULT4 and differ in their tissue distribution and substrate specificities. The most common donor molecule is 3’-phosphoadenosine-5’-phosphosulfate (PAP).
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'''Sulfotransferase''' (ST) are enzymes which catalyze the transfer of a sulfate group from a donor molecule to an acceptor alcohol or amine. The acceptors are hormones, neurotransmitters, drugs and xenobiotic compounds. The addition of a charged chemical moiety to the above carbon-rich water-insoluble molecules, make them more soluble and thus transportable in the circulatory system<ref>PMID:20136513</ref>. The various human STs are named SULT1, SULT2, SULT4 and differ in their tissue distribution and substrate specificities. The most common donor molecule is 3’-phosphoadenosine-5’-phosphosulfate ('''PAP''').
*'''Estrogen sulfotransferase''' sulfates estrogen to inactivate it. Involved in sulfation of thyroid hormones<ref>PMID:33799763</ref>.
*'''Estrogen sulfotransferase''' sulfates estrogen to inactivate it. Involved in sulfation of thyroid hormones<ref>PMID:33799763</ref>.
*'''Heparan sulphate sulfotransferase''' sulfates iduronic acid and glucosamine<ref>PMID:33102470</ref>.
*'''Heparan sulphate sulfotransferase''' sulfates iduronic acid and glucosamine<ref>PMID:33102470</ref>.

Revision as of 10:26, 14 August 2024

Human estrogen sulfotransferase dimer complex with cofactor PAP, 1hy3

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References

  1. ↑ Malojcic G, Glockshuber R. The PAPS-independent aryl sulfotransferase and the alternative disulfide bond formation system in pathogenic bacteria. Antioxid Redox Signal. 2010 Oct;13(8):1247-59. doi: 10.1089/ars.2010.3119. PMID:20136513 doi:http://dx.doi.org/10.1089/ars.2010.3119
  2. ↑ Yi M, Negishi M, Lee SJ. Estrogen Sulfotransferase (SULT1E1): Its Molecular Regulation, Polymorphisms, and Clinical Perspectives. J Pers Med. 2021 Mar 11;11(3):194. PMID:33799763 doi:10.3390/jpm11030194
  3. ↑ Teixeira FCOB, Vijaya Kumar A, Kumar Katakam S, Cocola C, Pelucchi P, Graf M, Kiesel L, Reinbold R, Pavão MSG, Greve B, Götte M. The Heparan Sulfate Sulfotransferases HS2ST1 and HS3ST2 Are Novel Regulators of Breast Cancer Stem-Cell Properties. Front Cell Dev Biol. 2020 Sep 25;8:559554. PMID:33102470 doi:10.3389/fcell.2020.559554
  4. ↑ Ouyang Yb, Lane WS, Moore KL. Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins. Proc Natl Acad Sci U S A. 1998 Mar 17;95(6):2896-901. PMID:9501187 doi:10.1073/pnas.95.6.2896
  5. ↑ Nagar S, Walther S, Blanchard RL. Sulfotransferase (SULT) 1A1 polymorphic variants *1, *2, and *3 are associated with altered enzymatic activity, cellular phenotype, and protein degradation. Mol Pharmacol. 2006 Jun;69(6):2084-92. PMID:16517757 doi:10.1124/mol.105.019240
  6. ↑ Engelke CE, Meinl W, Boeing H, Glatt H. Association between functional genetic polymorphisms of human sulfotransferases 1A1 and 1A2. Pharmacogenetics. 2000 Mar;10(2):163-9. PMID:10762004 doi:10.1097/00008571-200003000-00008
  7. ↑ Bian HS, Ngo SY, Tan W, Wong CH, Boelsterli UA, Tan TM. Induction of human sulfotransferase 1A3 (SULT1A3) by glucocorticoids. Life Sci. 2007 Dec 14;81(25-26):1659-67. PMID:17963788 doi:10.1016/j.lfs.2007.09.029
  8. ↑ Yalcin EB, More V, Neira KL, Lu ZJ, Cherrington NJ, Slitt AL, King RS. Downregulation of sulfotransferase expression and activity in diseased human livers. Drug Metab Dispos. 2013 Sep;41(9):1642-50. doi: 10.1124/dmd.113.050930. Epub 2013, Jun 17. PMID:23775849 doi:http://dx.doi.org/10.1124/dmd.113.050930
  9. ↑ Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M. Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction. J Biol Chem. 2002 May 17;277(20):17928-32. Epub 2002 Mar 7. PMID:11884392 doi:http://dx.doi.org/10.1074/jbc.M111651200

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