19055353

Source:http://linkedlifedata.com/resource/pubmed/id/19055353

Download in:

Switch to

Custom View

Named Graph Language Inference

Statements in which the resource exists as a subject.
Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0020792, umls-concept:C0020944, umls-concept:C0033684, umls-concept:C0205227, umls-concept:C0449445, umls-concept:C0870883, umls-concept:C1704675, umls-concept:C1880022
pubmed:issue	1
pubmed:dateCreated	2009-1-8
pubmed:abstractText	The emerging field of global mass-based metabolomics provides a platform for discovering unknown metabolites and their specific biochemical pathways. We report the identification of a new endogenous metabolite, N(4)-(N-acetylaminopropyl)spermidine and the use of a novel proteomics based method for the investigation of its protein interaction using metabolite immobilization on agarose beads. The metabolite was isolated from the organism Pyrococcus furiosus, and structurally characterized through an iterative process of synthesizing candidate molecules and comparative analysis using accurate mass LC-MS/MS. An approach developed for the selective preparation of N(1)-acetylthermospermine, one of the possible structures of the unknown metabolite, provides a convenient route to new polyamine derivatives through methylation on the N(8) and N(4) of the thermospermine scaffold. The biochemical role of the novel metabolite as well as that of two other polyamines: spermidine and agmatine is investigated through metabolite immobilization and incubation with native proteins. The identification of eleven proteins that uniquely bind with N(4)-(N-acetylaminopropyl)spermidine, provides information on the role of this novel metabolite in the native organism. Identified proteins included hypothetical ones such as PF0607 and PF1199, and those involved in translation, DNA synthesis and the urea cycle like translation initiation factor IF-2, 50S ribosomal protein L14e, DNA-directed RNA polymerase, and ornithine carbamoyltransferase. The immobilization approach demonstrated here has the potential for application to other newly discovered endogenous metabolites found through untargeted metabolomics, as a preliminary screen for generating a list of proteins that could be further investigated for specific activity.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/P30 MH062261, http://linkedlifedata.com/resource/pubmed/grant/P30 MH062261-05S1, http://linkedlifedata.com/resource/pubmed/grant/R24 EY017540, http://linkedlifedata.com/resource/pubmed/grant/R24 EY017540-02
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-10637415, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-10841484, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-11055357, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-11210495, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-12477358, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-12855657, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-15351398, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-15502846, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-15673283, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-15983049, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-16428316, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-17269703, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-17429571, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-18247545, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-18521184, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-2329556, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-479149, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-6206782, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-7050105, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-8113228, http://linkedlifedata.com/resource/pubmed/commentcorrection/19055353-8411017
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/7503056
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Spermidine
pubmed:status	MEDLINE
pubmed:month	Jan
pubmed:issn	1520-5126
pubmed:author	pubmed-author:AdamsMike W WMW, pubmed-author:FokinValery VVV, pubmed-author:KalisiakEwaE, pubmed-author:KalisiakJaros?awJ, pubmed-author:MoritaHirotoshiH, pubmed-author:SharplessK BarryKB, pubmed-author:SiuzdakGaryG, pubmed-author:TraugerSunia ASA
pubmed:issnType	Electronic
pubmed:day	14
pubmed:volume	131
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	378-86
pubmed:dateRevised	2010-12-3
pubmed:meshHeading	pubmed-meshheading:19055353-Metabolomics, pubmed-meshheading:19055353-Proteins, pubmed-meshheading:19055353-Pyrococcus furiosus, pubmed-meshheading:19055353-Spermidine, pubmed-meshheading:19055353-Tandem Mass Spectrometry
pubmed:year	2009
pubmed:articleTitle	Identification of a new endogenous metabolite and the characterization of its protein interactions through an immobilization approach.
pubmed:affiliation	Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural