Sulfotransferase
From Proteopedia
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| - | + | <StructureSection load='1hy3' size='450' side='right' scene='' caption='Human estrogen sulfotransferase dimer complex with cofactor PAP (stick model), [[1hy3]]'> | |
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== 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). | ||
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== Structural highlights == | == Structural highlights == | ||
ST catalytic residues His and Lys interact with the sulfate donor molecule PAP<ref>PMID:11884392</ref>. | ST catalytic residues His and Lys interact with the sulfate donor molecule PAP<ref>PMID:11884392</ref>. | ||
| - | + | </StructureSection> | |
==3D structures of sulfotransferase== | ==3D structures of sulfotransferase== | ||
Revision as of 11:13, 4 September 2016
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3D structures of sulfotransferase
Updated on 04-September-2016
References
- ↑ 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
- ↑ 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
- ↑ 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
