| pubmed-article:15240249 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15240249 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:15240249 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:15240249 | lifeskim:mentions | umls-concept:C0032214 | lld:lifeskim |
| pubmed-article:15240249 | lifeskim:mentions | umls-concept:C0600138 | lld:lifeskim |
| pubmed-article:15240249 | lifeskim:mentions | umls-concept:C0076464 | lld:lifeskim |
| pubmed-article:15240249 | lifeskim:mentions | umls-concept:C0033268 | lld:lifeskim |
| pubmed-article:15240249 | lifeskim:mentions | umls-concept:C0067075 | lld:lifeskim |
| pubmed-article:15240249 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:15240249 | pubmed:dateCreated | 2004-7-8 | lld:pubmed |
| pubmed-article:15240249 | pubmed:abstractText | 3-Hydroxydecanoic acid (3HD) was produced in Escherichia coli by mobilizing (R)-3-hydroxydecanoyl-acyl carrier protein-coenzyme A transacylase (PhaG, encoded by the phaG gene). By employing an isogenic tesB (encoding thioesterase II)-negative knockout E. coli strain, CH01, it was found that the expressions of tesB and phaG can up-regulate each other. In addition, 3HD was synthesized from glucose or fructose by recombinant E. coli harboring phaG and tesB. This study supports the hypothesis that the physiological role of thioesterase II in E. coli is to prevent the abnormal accumulation of intracellular acyl-coenzyme A. | lld:pubmed |
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| pubmed-article:15240249 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15240249 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15240249 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15240249 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15240249 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:15240249 | pubmed:issn | 0099-2240 | lld:pubmed |
| pubmed-article:15240249 | pubmed:author | pubmed-author:LeeD BDB | lld:pubmed |
| pubmed-article:15240249 | pubmed:author | pubmed-author:ChenGuo-Qiang... | lld:pubmed |
| pubmed-article:15240249 | pubmed:author | pubmed-author:ZAKR LRL | lld:pubmed |
| pubmed-article:15240249 | pubmed:author | pubmed-author:DengYingY | lld:pubmed |
| pubmed-article:15240249 | pubmed:author | pubmed-author:ChenJin-ChunJ... | lld:pubmed |
| pubmed-article:15240249 | pubmed:author | pubmed-author:GongQiangQ | lld:pubmed |
| pubmed-article:15240249 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15240249 | pubmed:volume | 70 | lld:pubmed |
| pubmed-article:15240249 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15240249 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15240249 | pubmed:pagination | 3807-13 | lld:pubmed |
| pubmed-article:15240249 | pubmed:dateRevised | 2010-9-21 | lld:pubmed |
| pubmed-article:15240249 | pubmed:meshHeading | pubmed-meshheading:15240249... | lld:pubmed |
| pubmed-article:15240249 | pubmed:meshHeading | pubmed-meshheading:15240249... | lld:pubmed |
| pubmed-article:15240249 | pubmed:meshHeading | pubmed-meshheading:15240249... | lld:pubmed |
| pubmed-article:15240249 | pubmed:meshHeading | pubmed-meshheading:15240249... | lld:pubmed |
| pubmed-article:15240249 | pubmed:meshHeading | pubmed-meshheading:15240249... | lld:pubmed |
| pubmed-article:15240249 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15240249 | pubmed:articleTitle | Thioesterase II of Escherichia coli plays an important role in 3-hydroxydecanoic acid production. | lld:pubmed |
| pubmed-article:15240249 | pubmed:affiliation | MOE Laboratory of Protein Science, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China. | lld:pubmed |
| pubmed-article:15240249 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15240249 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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