| pubmed-article:19188064 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19188064 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:19188064 | lifeskim:mentions | umls-concept:C0071598 | lld:lifeskim |
| pubmed-article:19188064 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
| pubmed-article:19188064 | lifeskim:mentions | umls-concept:C0597572 | lld:lifeskim |
| pubmed-article:19188064 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:19188064 | pubmed:dateCreated | 2009-2-23 | lld:pubmed |
| pubmed-article:19188064 | pubmed:abstractText | Polyketide synthase (PKS) thioesterases (TEs) catalyze the macrocyclization of linear acyl chains into macrolactones. Herein we show that peptide based substrates are processed by PKS TEs with greater catalytic efficiency than more native like acyl substrates. This result strengths the link between PKS and non-ribosomal peptide synthetase systems and provides a new tool for studying PKS TEs. | lld:pubmed |
| pubmed-article:19188064 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19188064 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19188064 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19188064 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19188064 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19188064 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19188064 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19188064 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:19188064 | pubmed:issn | 1464-3405 | lld:pubmed |
| pubmed-article:19188064 | pubmed:author | pubmed-author:WangMengM | lld:pubmed |
| pubmed-article:19188064 | pubmed:author | pubmed-author:BoddyChristop... | lld:pubmed |
| pubmed-article:19188064 | pubmed:author | pubmed-author:OparePeterP | lld:pubmed |
| pubmed-article:19188064 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19188064 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:19188064 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:19188064 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19188064 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19188064 | pubmed:pagination | 1413-5 | lld:pubmed |
| pubmed-article:19188064 | pubmed:meshHeading | pubmed-meshheading:19188064... | lld:pubmed |
| pubmed-article:19188064 | pubmed:meshHeading | pubmed-meshheading:19188064... | lld:pubmed |
| pubmed-article:19188064 | pubmed:meshHeading | pubmed-meshheading:19188064... | lld:pubmed |
| pubmed-article:19188064 | pubmed:meshHeading | pubmed-meshheading:19188064... | lld:pubmed |
| pubmed-article:19188064 | pubmed:meshHeading | pubmed-meshheading:19188064... | lld:pubmed |
| pubmed-article:19188064 | pubmed:meshHeading | pubmed-meshheading:19188064... | lld:pubmed |
| pubmed-article:19188064 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19188064 | pubmed:articleTitle | Polyketide synthase thioesterases catalyze rapid hydrolysis of peptidyl thioesters. | lld:pubmed |
| pubmed-article:19188064 | pubmed:affiliation | Department of Chemistry, Syracuse University, Syracuse, NY 13244-4100, USA. | lld:pubmed |
| pubmed-article:19188064 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19188064 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:19188064 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:19188064 | lld:chembl |
