pubmed-article:20647463 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20647463 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
pubmed-article:20647463 | lifeskim:mentions | umls-concept:C1516769 | lld:lifeskim |
pubmed-article:20647463 | lifeskim:mentions | umls-concept:C0765250 | lld:lifeskim |
pubmed-article:20647463 | lifeskim:mentions | umls-concept:C0175921 | lld:lifeskim |
pubmed-article:20647463 | lifeskim:mentions | umls-concept:C1880157 | lld:lifeskim |
pubmed-article:20647463 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
pubmed-article:20647463 | pubmed:issue | 5989 | lld:pubmed |
pubmed-article:20647463 | pubmed:dateCreated | 2010-7-21 | lld:pubmed |
pubmed-article:20647463 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20647463 | pubmed:abstractText | The Diels-Alder reaction is a cornerstone in organic synthesis, forming two carbon-carbon bonds and up to four new stereogenic centers in one step. No naturally occurring enzymes have been shown to catalyze bimolecular Diels-Alder reactions. We describe the de novo computational design and experimental characterization of enzymes catalyzing a bimolecular Diels-Alder reaction with high stereoselectivity and substrate specificity. X-ray crystallography confirms that the structure matches the design for the most active of the enzymes, and binding site substitutions reprogram the substrate specificity. Designed stereoselective catalysts for carbon-carbon bond-forming reactions should be broadly useful in synthetic chemistry. | lld:pubmed |
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pubmed-article:20647463 | pubmed:language | eng | lld:pubmed |
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pubmed-article:20647463 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20647463 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:20647463 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20647463 | pubmed:month | Jul | lld:pubmed |
pubmed-article:20647463 | pubmed:issn | 1095-9203 | lld:pubmed |
pubmed-article:20647463 | pubmed:author | pubmed-author:KudaJJ | lld:pubmed |
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pubmed-article:20647463 | pubmed:author | pubmed-author:MichaelForres... | lld:pubmed |
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pubmed-article:20647463 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20647463 | pubmed:day | 16 | lld:pubmed |
pubmed-article:20647463 | pubmed:volume | 329 | lld:pubmed |
pubmed-article:20647463 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20647463 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20647463 | pubmed:pagination | 309-13 | lld:pubmed |
pubmed-article:20647463 | pubmed:dateRevised | 2011-1-5 | lld:pubmed |
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pubmed-article:20647463 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20647463 | pubmed:articleTitle | Computational design of an enzyme catalyst for a stereoselective bimolecular Diels-Alder reaction. | lld:pubmed |
pubmed-article:20647463 | pubmed:affiliation | Department of Biochemistry, University of Washington, Seattle, WA 98195, USA. | lld:pubmed |
pubmed-article:20647463 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20647463 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:20647463 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:20647463 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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