| pubmed-article:2835095 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2835095 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:2835095 | lifeskim:mentions | umls-concept:C0031705 | lld:lifeskim |
| pubmed-article:2835095 | lifeskim:mentions | umls-concept:C1260231 | lld:lifeskim |
| pubmed-article:2835095 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:2835095 | lifeskim:mentions | umls-concept:C0750729 | lld:lifeskim |
| pubmed-article:2835095 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:2835095 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:2835095 | pubmed:dateCreated | 1988-6-14 | lld:pubmed |
| pubmed-article:2835095 | pubmed:abstractText | The reaction mechanism for the phosphotriesterase from Pseudomonas diminuta has been examined. When paraoxon (diethyl 4-nitrophenyl phosphate) is hydrolyzed by this enzyme in oxygen-18-labeled water, the oxygen-18 label is found exclusively in the diethyl phosphate product. The absolute configurations for the (+) and (-) enantiomers of O-ethyl phenylphosphonothioic acid have been determined by X-ray diffraction structural determination of the individual crystalline 1-phenylethylamine salts. The (+) enantiomer of the free acid corresponds to the RP configuration. The RP enantiomer of O-ethyl phenylphosphonothioic acid has been converted to the SP enantiomer of EPN [O-ethyl O-(4-nitrophenyl) phenylphosphonothioate]. (SP)-EPN is hydrolyzed by the phosphotriesterase to the SP enantiomer of O-ethyl phenylphosphonothioic acid. The enzymatic reaction therefore proceeds with inversion of configuration. These results have been interpreted as an indication of a single in-line displacement by an activated water molecule directly at the phosphorus center of the phosphotriester substrate. (RP)-EPN is not hydrolyzed by the enzyme at an appreciable rate. | lld:pubmed |
| pubmed-article:2835095 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835095 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2835095 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835095 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2835095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835095 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2835095 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:2835095 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:2835095 | pubmed:author | pubmed-author:WildJ RJR | lld:pubmed |
| pubmed-article:2835095 | pubmed:author | pubmed-author:RaushelF MFM | lld:pubmed |
| pubmed-article:2835095 | pubmed:author | pubmed-author:LewisV EVE | lld:pubmed |
| pubmed-article:2835095 | pubmed:author | pubmed-author:DonarskiW JWJ | lld:pubmed |
| pubmed-article:2835095 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2835095 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:2835095 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:2835095 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2835095 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2835095 | pubmed:pagination | 1591-7 | lld:pubmed |
| pubmed-article:2835095 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:2835095 | pubmed:meshHeading | pubmed-meshheading:2835095-... | lld:pubmed |
| pubmed-article:2835095 | pubmed:meshHeading | pubmed-meshheading:2835095-... | lld:pubmed |
| pubmed-article:2835095 | pubmed:meshHeading | pubmed-meshheading:2835095-... | lld:pubmed |
| pubmed-article:2835095 | pubmed:meshHeading | pubmed-meshheading:2835095-... | lld:pubmed |
| pubmed-article:2835095 | pubmed:meshHeading | pubmed-meshheading:2835095-... | lld:pubmed |
| pubmed-article:2835095 | pubmed:meshHeading | pubmed-meshheading:2835095-... | lld:pubmed |
| pubmed-article:2835095 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2835095 | pubmed:articleTitle | Mechanism and stereochemical course at phosphorus of the reaction catalyzed by a bacterial phosphotriesterase. | lld:pubmed |
| pubmed-article:2835095 | pubmed:affiliation | Department of Chemistry, Texas A&M University, College Station 77843. | lld:pubmed |
| pubmed-article:2835095 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2835095 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2835095 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2835095 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2835095 | lld:pubmed |
