| pubmed-article:19530704 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19530704 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:19530704 | lifeskim:mentions | umls-concept:C0071598 | lld:lifeskim |
| pubmed-article:19530704 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:19530704 | lifeskim:mentions | umls-concept:C0032214 | lld:lifeskim |
| pubmed-article:19530704 | lifeskim:mentions | umls-concept:C0521033 | lld:lifeskim |
| pubmed-article:19530704 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
| pubmed-article:19530704 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:19530704 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:19530704 | lifeskim:mentions | umls-concept:C2828360 | lld:lifeskim |
| pubmed-article:19530704 | pubmed:issue | 27 | lld:pubmed |
| pubmed-article:19530704 | pubmed:dateCreated | 2009-7-7 | lld:pubmed |
| pubmed-article:19530704 | pubmed:abstractText | Zearalenone, a fungal macrocyclic polyketide, is a member of the resorcylic acid lactone family. Herein, we characterize in vitro the thioesterase from PKS13 in zearalenone biosynthesis (Zea TE). The excised Zea TE catalyzes macrocyclization of a linear thioester-activated model of zearalenone. Zea TE also catalyzes the cross coupling of a benzoyl thioester with alcohols and amines. Kinetic characterization of the cross coupling is consistent with a ping-pong bi-bi mechanism, confirming an acyl-enzyme intermediate. Finally, the substrate specificity of the Zea TE indicates the TE may help control iterative cycling on PKS13 by rapidly offloading the final resorcylate-containing product. | lld:pubmed |
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| pubmed-article:19530704 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19530704 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19530704 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19530704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19530704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19530704 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19530704 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:19530704 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:19530704 | pubmed:author | pubmed-author:ZhouHuiH | lld:pubmed |
| pubmed-article:19530704 | pubmed:author | pubmed-author:TangYiY | lld:pubmed |
| pubmed-article:19530704 | pubmed:author | pubmed-author:WangMengM | lld:pubmed |
| pubmed-article:19530704 | pubmed:author | pubmed-author:BoddyChristop... | lld:pubmed |
| pubmed-article:19530704 | pubmed:author | pubmed-author:WirzMonicaM | lld:pubmed |
| pubmed-article:19530704 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19530704 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:19530704 | pubmed:volume | 48 | lld:pubmed |
| pubmed-article:19530704 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19530704 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19530704 | pubmed:pagination | 6288-90 | lld:pubmed |
| pubmed-article:19530704 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
| pubmed-article:19530704 | pubmed:meshHeading | pubmed-meshheading:19530704... | lld:pubmed |
| pubmed-article:19530704 | pubmed:meshHeading | pubmed-meshheading:19530704... | lld:pubmed |
| pubmed-article:19530704 | pubmed:meshHeading | pubmed-meshheading:19530704... | lld:pubmed |
| pubmed-article:19530704 | pubmed:meshHeading | pubmed-meshheading:19530704... | lld:pubmed |
| pubmed-article:19530704 | pubmed:meshHeading | pubmed-meshheading:19530704... | lld:pubmed |
| pubmed-article:19530704 | pubmed:meshHeading | pubmed-meshheading:19530704... | lld:pubmed |
| pubmed-article:19530704 | pubmed:meshHeading | pubmed-meshheading:19530704... | lld:pubmed |
| pubmed-article:19530704 | pubmed:meshHeading | pubmed-meshheading:19530704... | lld:pubmed |
| pubmed-article:19530704 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19530704 | pubmed:articleTitle | A thioesterase from an iterative fungal polyketide synthase shows macrocyclization and cross coupling activity and may play a role in controlling iterative cycling through product offloading. | lld:pubmed |
| pubmed-article:19530704 | pubmed:affiliation | Department of Chemistry, University of Ottawa, Ottawa, ON, Canada T1N 6N5. | lld:pubmed |
| pubmed-article:19530704 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19530704 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19530704 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
