| pubmed-article:6296110 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6296110 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:6296110 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:6296110 | lifeskim:mentions | umls-concept:C0750729 | lld:lifeskim |
| pubmed-article:6296110 | lifeskim:mentions | umls-concept:C0597094 | lld:lifeskim |
| pubmed-article:6296110 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:6296110 | pubmed:dateCreated | 1983-3-17 | lld:pubmed |
| pubmed-article:6296110 | pubmed:abstractText | Nuclease S1 hydrolyzes the Sp-diastereomer of 5'-O-(2'-deoxyadenosyl)-3'-O-thymidyl phosphorothioate in H2(18)O to [18O]deoxyadenosine 5'-O-phosphorothioate which can be phosphorylated enzymatically to the Sp-diastereomer of [alpha-18O]deoxyadenosine 5'-O-(1-thiotriphosphate). 31P nmr spectroscopy shows the oxygen-18 in this compound to be in a nonbridging position at the alpha-phosphorus, indicating that the hydrolysis reaction catalyzed by nuclease S1 proceeds with inversion of configuration at phosphorus. This result is compatible with a direct nucleophilic attack of H2O at phosphorus without the involvement of a covalent enzyme intermediate. | lld:pubmed |
| pubmed-article:6296110 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6296110 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6296110 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6296110 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:6296110 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6296110 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:6296110 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:6296110 | pubmed:author | pubmed-author:EcksteinFF | lld:pubmed |
| pubmed-article:6296110 | pubmed:author | pubmed-author:RomaniukP JPJ | lld:pubmed |
| pubmed-article:6296110 | pubmed:author | pubmed-author:PotterB VBV | lld:pubmed |
| pubmed-article:6296110 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6296110 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:6296110 | pubmed:volume | 258 | lld:pubmed |
| pubmed-article:6296110 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6296110 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6296110 | pubmed:pagination | 1758-60 | lld:pubmed |
| pubmed-article:6296110 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:6296110 | pubmed:meshHeading | pubmed-meshheading:6296110-... | lld:pubmed |
| pubmed-article:6296110 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6296110 | pubmed:articleTitle | Stereochemical course of DNA hydrolysis by nuclease S1. | lld:pubmed |
| pubmed-article:6296110 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6296110 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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