| pubmed-article:10860985 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10860985 | lifeskim:mentions | umls-concept:C0315140 | lld:lifeskim |
| pubmed-article:10860985 | lifeskim:mentions | umls-concept:C0025519 | lld:lifeskim |
| pubmed-article:10860985 | lifeskim:mentions | umls-concept:C0034140 | lld:lifeskim |
| pubmed-article:10860985 | lifeskim:mentions | umls-concept:C0020364 | lld:lifeskim |
| pubmed-article:10860985 | lifeskim:mentions | umls-concept:C0043316 | lld:lifeskim |
| pubmed-article:10860985 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:10860985 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:10860985 | lifeskim:mentions | umls-concept:C0220903 | lld:lifeskim |
| pubmed-article:10860985 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:10860985 | pubmed:dateCreated | 2000-7-31 | lld:pubmed |
| pubmed-article:10860985 | pubmed:abstractText | During purification of the selenium-dependent xanthine dehydrogenase (XDH) from Clostridium purinolyticum, another hydroxylase was uncovered that also contained selenium and exhibited similar spectral properties. This enzyme was purified to homogeneity. It uses purine, 2OH-purine, and hypoxanthine as substrates, and based on its substrate specificity, this selenoenzyme is termed purine hydroxylase (PH). The product of hydroxylation of purine by PH is xanthine. A concomitant release of selenium from the enzyme and loss of catalytic activity on treatment with cyanide indicates that selenium is essential for PH activity. Selenium-dependent XDH, also purified from C. purinolyticum, was found to be insensitive to oxygen during purification and to use both potassium ferricyanide and 2,6-dichloroindophenol as electron acceptors. Selenium is required for the xanthine-dependent reduction of 2, 6-dichloroindophenol by XDH. Kinetic analyses of both enzymes revealed that xanthine is the preferred substrate for XDH and purine and hypoxanthine are preferred by PH. This characterization of these selenium-requiring hydroxylases involved in the interconversion of purines describes an extension of the pathway for purine fermentation in the purinolytic clostridia. | lld:pubmed |
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| pubmed-article:10860985 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10860985 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10860985 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10860985 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10860985 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10860985 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10860985 | pubmed:author | pubmed-author:StadtmanT CTC | lld:pubmed |
| pubmed-article:10860985 | pubmed:author | pubmed-author:SelfW TWT | lld:pubmed |
| pubmed-article:10860985 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10860985 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:10860985 | pubmed:volume | 97 | lld:pubmed |
| pubmed-article:10860985 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10860985 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10860985 | pubmed:pagination | 7208-13 | lld:pubmed |
| pubmed-article:10860985 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10860985 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10860985 | pubmed:articleTitle | Selenium-dependent metabolism of purines: A selenium-dependent purine hydroxylase and xanthine dehydrogenase were purified from Clostridium purinolyticum and characterized. | lld:pubmed |
| pubmed-article:10860985 | pubmed:affiliation | Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. | lld:pubmed |
| pubmed-article:10860985 | pubmed:publicationType | Journal Article | lld:pubmed |
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