19188064

Source:http://linkedlifedata.com/resource/pubmed/id/19188064

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0020291, umls-concept:C0071598, umls-concept:C0439831, umls-concept:C0597572
pubmed:issue	5
pubmed:dateCreated	2009-2-23
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.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9107377
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Esters, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Polyketide Synthases
pubmed:status	MEDLINE
pubmed:month	Mar
pubmed:issn	1464-3405
pubmed:author	pubmed-author:BoddyChristopher NCN, pubmed-author:OparePeterP, pubmed-author:WangMengM
pubmed:issnType	Electronic
pubmed:day	1
pubmed:volume	19
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1413-5
pubmed:meshHeading	pubmed-meshheading:19188064-Catalysis, pubmed-meshheading:19188064-Esterification, pubmed-meshheading:19188064-Esters, pubmed-meshheading:19188064-Hydrolysis, pubmed-meshheading:19188064-Peptides, pubmed-meshheading:19188064-Polyketide Synthases
pubmed:year	2009
pubmed:articleTitle	Polyketide synthase thioesterases catalyze rapid hydrolysis of peptidyl thioesters.
pubmed:affiliation	Department of Chemistry, Syracuse University, Syracuse, NY 13244-4100, USA.
pubmed:publicationType	Journal Article, Comparative Study, Research Support, Non-U.S. Gov't