| pubmed-article:20433174 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20433174 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:20433174 | lifeskim:mentions | umls-concept:C0022023 | lld:lifeskim |
| pubmed-article:20433174 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:20433174 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:20433174 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:20433174 | lifeskim:mentions | umls-concept:C0077943 | lld:lifeskim |
| pubmed-article:20433174 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:20433174 | lifeskim:mentions | umls-concept:C0596455 | lld:lifeskim |
| pubmed-article:20433174 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:20433174 | pubmed:dateCreated | 2010-5-20 | lld:pubmed |
| pubmed-article:20433174 | pubmed:abstractText | The purple acid phosphatases (PAP) are binuclear metallohydrolases that catalyze the hydrolysis of a broad range of phosphomonoester substrates. The mode of substrate binding during catalysis and the identity of the nucleophile is subject to debate. Here, we used native Fe(3+)-Fe(2+) pig PAP (uteroferrin; Uf) and its Fe(3+)-Mn(2+) derivative to investigate the effect of metal ion substitution on the mechanism of catalysis. Replacement of the Fe(2+) by Mn(2+) lowers the reactivity of Uf. However, using stopped-flow measurements it could be shown that this replacement facilitates approximately a ten-fold faster reaction between both substrate and inorganic phosphate with the chromophoric Fe(3+) site. These data also indicate that in both metal forms of Uf, phenyl phosphate hydrolysis occurs faster than formation of a mu-1,3 phosphate complex. The slower rate of interaction between substrate and the Fe(3+) site relative to catalysis suggests that the substrate is hydrolyzed while coordinated only to the divalent metal ion. The likely nucleophile is a water molecule in the second coordination sphere, activated by a hydroxide terminally coordinated to Fe(3+). The faster rates of interaction with the Fe(3+) site in the Fe(3+)-Mn(2+) derivative than the native Fe(3+)-Fe(2+) form are likely mediated via a hydrogen bond network connecting the first and second coordination spheres, and illustrate how the selection of metal ions may be important in fine-tuning the function of this enzyme. | lld:pubmed |
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| pubmed-article:20433174 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20433174 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20433174 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20433174 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20433174 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20433174 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20433174 | pubmed:month | May | lld:pubmed |
| pubmed-article:20433174 | pubmed:issn | 1520-5126 | lld:pubmed |
| pubmed-article:20433174 | pubmed:author | pubmed-author:HenggeAlvan... | lld:pubmed |
| pubmed-article:20433174 | pubmed:author | pubmed-author:GahanLawrence... | lld:pubmed |
| pubmed-article:20433174 | pubmed:author | pubmed-author:Miti?NatasaN | lld:pubmed |
| pubmed-article:20433174 | pubmed:author | pubmed-author:SchenkGerhard... | lld:pubmed |
| pubmed-article:20433174 | pubmed:author | pubmed-author:HadlerKieran... | lld:pubmed |
| pubmed-article:20433174 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20433174 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:20433174 | pubmed:volume | 132 | lld:pubmed |
| pubmed-article:20433174 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20433174 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20433174 | pubmed:pagination | 7049-54 | lld:pubmed |
| pubmed-article:20433174 | pubmed:dateRevised | 2011-7-28 | lld:pubmed |
| pubmed-article:20433174 | pubmed:meshHeading | pubmed-meshheading:20433174... | lld:pubmed |
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| pubmed-article:20433174 | pubmed:meshHeading | pubmed-meshheading:20433174... | lld:pubmed |
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| pubmed-article:20433174 | pubmed:meshHeading | pubmed-meshheading:20433174... | lld:pubmed |
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| pubmed-article:20433174 | pubmed:meshHeading | pubmed-meshheading:20433174... | lld:pubmed |
| pubmed-article:20433174 | pubmed:meshHeading | pubmed-meshheading:20433174... | lld:pubmed |
| pubmed-article:20433174 | pubmed:meshHeading | pubmed-meshheading:20433174... | lld:pubmed |
| pubmed-article:20433174 | pubmed:meshHeading | pubmed-meshheading:20433174... | lld:pubmed |
| pubmed-article:20433174 | pubmed:meshHeading | pubmed-meshheading:20433174... | lld:pubmed |
| pubmed-article:20433174 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20433174 | pubmed:articleTitle | The divalent metal ion in the active site of uteroferrin modulates substrate binding and catalysis. | lld:pubmed |
| pubmed-article:20433174 | pubmed:affiliation | School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland, 4072, Australia. | lld:pubmed |
| pubmed-article:20433174 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20433174 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20433174 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:397414 | entrezgene:pubmed | pubmed-article:20433174 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20433174 | lld:entrezgene |
