| pubmed-article:16707489 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16707489 | lifeskim:mentions | umls-concept:C0521026 | lld:lifeskim |
| pubmed-article:16707489 | lifeskim:mentions | umls-concept:C0040085 | lld:lifeskim |
| pubmed-article:16707489 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:16707489 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16707489 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:16707489 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:16707489 | pubmed:dateCreated | 2006-8-14 | lld:pubmed |
| pubmed-article:16707489 | pubmed:abstractText | By using biochemical and structural analyses, we have investigated the catalytic mechanism of the recently discovered flavin-dependent thymidylate synthase ThyX from Paramecium bursaria chlorella virus-1 (PBCV-1). Site-directed mutagenesis experiments have identified several residues implicated in either NADPH oxidation or deprotonation activity of PBCV-1 ThyX. Chemical modification by diethyl pyrocarbonate and mass spectroscopic analyses identified a histidine residue (His53) crucial for NADPH oxidation and located in the vicinity of the redox active N-5 atom of the FAD ring system. Moreover, we observed that the conformation of active site key residues of PBCV-1 ThyX differs from earlier reported ThyX structures, suggesting structural changes during catalysis. Steady-state kinetic analyses support a reaction mechanism where ThyX catalysis proceeds via formation of distinct ternary complexes without formation of a methyl enzyme intermediate. | lld:pubmed |
| pubmed-article:16707489 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16707489 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16707489 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16707489 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16707489 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16707489 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16707489 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16707489 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16707489 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16707489 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:16707489 | pubmed:author | pubmed-author:MarchandChris... | lld:pubmed |
| pubmed-article:16707489 | pubmed:author | pubmed-author:DecottigniesP... | lld:pubmed |
| pubmed-article:16707489 | pubmed:author | pubmed-author:LieblUrsulaU | lld:pubmed |
| pubmed-article:16707489 | pubmed:author | pubmed-author:MyllykallioHa... | lld:pubmed |
| pubmed-article:16707489 | pubmed:author | pubmed-author:GrailleMarcM | lld:pubmed |
| pubmed-article:16707489 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:16707489 | pubmed:author | pubmed-author:ZhouCong-Zhao... | lld:pubmed |
| pubmed-article:16707489 | pubmed:author | pubmed-author:SkouloubrisSt... | lld:pubmed |
| pubmed-article:16707489 | pubmed:author | pubmed-author:GrazianiSébas... | lld:pubmed |
| pubmed-article:16707489 | pubmed:author | pubmed-author:BernauerJulie... | lld:pubmed |
| pubmed-article:16707489 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16707489 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:16707489 | pubmed:volume | 281 | lld:pubmed |
| pubmed-article:16707489 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16707489 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16707489 | pubmed:pagination | 24048-57 | lld:pubmed |
| pubmed-article:16707489 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:16707489 | pubmed:meshHeading | pubmed-meshheading:16707489... | lld:pubmed |
| pubmed-article:16707489 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16707489 | pubmed:articleTitle | Catalytic mechanism and structure of viral flavin-dependent thymidylate synthase ThyX. | lld:pubmed |
| pubmed-article:16707489 | pubmed:affiliation | CNRS, UMR 7645, Laboratory of Optics and Biosciences, Ecole Polytechnique, 91128 Palaiseau, France. | lld:pubmed |
| pubmed-article:16707489 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16707489 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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