| pubmed-article:21111704 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21111704 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:21111704 | lifeskim:mentions | umls-concept:C0597538 | lld:lifeskim |
| pubmed-article:21111704 | lifeskim:mentions | umls-concept:C1423108 | lld:lifeskim |
| pubmed-article:21111704 | lifeskim:mentions | umls-concept:C1413945 | lld:lifeskim |
| pubmed-article:21111704 | lifeskim:mentions | umls-concept:C1452189 | lld:lifeskim |
| pubmed-article:21111704 | lifeskim:mentions | umls-concept:C1422804 | lld:lifeskim |
| pubmed-article:21111704 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
| pubmed-article:21111704 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
| pubmed-article:21111704 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:21111704 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:21111704 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:21111704 | pubmed:dateCreated | 2011-1-28 | lld:pubmed |
| pubmed-article:21111704 | 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. | lld:pubmed |
| pubmed-article:21111704 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21111704 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21111704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21111704 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21111704 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:21111704 | pubmed:issn | 1096-0384 | lld:pubmed |
| pubmed-article:21111704 | pubmed:author | pubmed-author:ChenGuangping... | lld:pubmed |
| pubmed-article:21111704 | pubmed:author | pubmed-author:CookPaul FPF | lld:pubmed |
| pubmed-article:21111704 | pubmed:author | pubmed-author:KumarVidya... | lld:pubmed |
| pubmed-article:21111704 | pubmed:author | pubmed-author:TyapochkinEdu... | lld:pubmed |
| pubmed-article:21111704 | pubmed:copyrightInfo | Copyright © 2010 Elsevier Inc. All rights reserved. | lld:pubmed |
| pubmed-article:21111704 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21111704 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:21111704 | pubmed:volume | 506 | lld:pubmed |
| pubmed-article:21111704 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21111704 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21111704 | pubmed:pagination | 137-41 | lld:pubmed |
| pubmed-article:21111704 | pubmed:dateRevised | 2011-10-6 | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:meshHeading | pubmed-meshheading:21111704... | lld:pubmed |
| pubmed-article:21111704 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21111704 | pubmed:articleTitle | Reaction product affinity regulates activation of human sulfotransferase 1A1 PAP sulfation. | lld:pubmed |
| pubmed-article:21111704 | pubmed:affiliation | Department of Physiological Sciences, Center for Veterinary Health Sciences, Oklahoma State University, Stillwater, OK 74078, USA. | lld:pubmed |
| pubmed-article:21111704 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21111704 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:21111704 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21111704 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:6817 | entrezgene:pubmed | pubmed-article:21111704 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21111704 | lld:entrezgene |
