Source:http://linkedlifedata.com/resource/pubmed/id/21111704
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2011-1-28
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| pubmed:abstractText |
Cytosolic sulfotransferase (SULT)-catalyzed sulfation regulates the activity of bio-signaling molecules and aids in metabolizing hydroxyl-containing xenobiotics. The sulfuryl donor for the SULT reaction is adenosine 3'-phosphate 5'-phosphosulfate (PAPS), while products are adenosine 3',5'-diphosphate (PAP) and a sulfated alcohol. Human phenol sulfotransferase (SULT1A1) is one of the major detoxifying enzymes for phenolic xenobiotics. The mechanism of SULT1A1-catalyzed sulfation of PAP by pNPS was investigated. PAP was sulfated by para-nitrophenyl sulfate (pNPS) in a concentration-dependent manner. 2-Naphthol inhibited sulfation of PAP, competing with pNPS, while phenol activated the sulfation reaction. At saturating PAP, a ping pong kinetic mechanism is observed with pNPS and phenol as substrates, consistent with phenol intercepting the E-PAPS complex prior to dissociation of PAPS. At high concentrations, phenol competes with pNPS, consistent with formation of the E-PAP-phenol dead-end complex. Data are consistent with the previously reported mechanism for sulfation of 2-naphthol by PAPS, and its activation by pNPS. Overall, data are consistent with release of PAP from E-PAP and PAPS from E-PAPS contributing to rate-limitation in both reaction directions.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-naphthol,
http://linkedlifedata.com/resource/pubmed/chemical/4-nitrophenyl sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Arylsulfotransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Naphthols,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrobenzenes,
http://linkedlifedata.com/resource/pubmed/chemical/Phenol,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoadenosine Phosphosulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SULT1A1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/adenosine 3'-phosphate-5'-phosphate
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
|
| pubmed:issn |
1096-0384
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright © 2010 Elsevier Inc. All rights reserved.
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| pubmed:issnType |
Electronic
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| pubmed:day |
15
|
| pubmed:volume |
506
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
137-41
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| pubmed:dateRevised |
2011-10-6
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| pubmed:meshHeading |
pubmed-meshheading:21111704-Adenosine Diphosphate,
pubmed-meshheading:21111704-Arylsulfotransferase,
pubmed-meshheading:21111704-Enzyme Activation,
pubmed-meshheading:21111704-Enzyme Inhibitors,
pubmed-meshheading:21111704-Humans,
pubmed-meshheading:21111704-Kinetics,
pubmed-meshheading:21111704-Models, Biological,
pubmed-meshheading:21111704-Naphthols,
pubmed-meshheading:21111704-Nitrobenzenes,
pubmed-meshheading:21111704-Phenol,
pubmed-meshheading:21111704-Phosphoadenosine Phosphosulfate,
pubmed-meshheading:21111704-Recombinant Fusion Proteins,
pubmed-meshheading:21111704-Substrate Specificity
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| pubmed:year |
2011
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| pubmed:articleTitle |
Reaction product affinity regulates activation of human sulfotransferase 1A1 PAP sulfation.
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| pubmed:affiliation |
Department of Physiological Sciences, Center for Veterinary Health Sciences, Oklahoma State University, Stillwater, OK 74078, USA.
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| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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