Sulfotransferase

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<StructureSection load='1hy3' size='450' side='right' scene='49/491888/Cv/2' caption='Human estrogen sulfotransferase dimer complex with cofactor PAP, [[1hy3]]'>
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<StructureSection load='' size='450' side='right' scene='49/491888/Cv/2' caption='Human estrogen sulfotransferase dimer complex with cofactor PAP, [[1hy3]]'>
== Function ==
== Function ==
'''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 SULT### and differ in their tissue distribution and substrate specificities. The most common donor molecule is 3’-phosphoadenosine-5’-phosphosulfate (PAP).
'''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 SULT### and differ in their tissue distribution and substrate specificities. The most common donor molecule is 3’-phosphoadenosine-5’-phosphosulfate (PAP).

Revision as of 12:45, 9 October 2017

Human estrogen sulfotransferase dimer complex with cofactor PAP, 1hy3

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3D structures of sulfotransferase

Updated on 09-October-2017

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. 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
  3. 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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