| pubmed-article:18571500 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18571500 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
| pubmed-article:18571500 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:18571500 | lifeskim:mentions | umls-concept:C0332255 | lld:lifeskim |
| pubmed-article:18571500 | lifeskim:mentions | umls-concept:C1414024 | lld:lifeskim |
| pubmed-article:18571500 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:18571500 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
| pubmed-article:18571500 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:18571500 | pubmed:dateCreated | 2008-7-22 | lld:pubmed |
| pubmed-article:18571500 | pubmed:abstractText | A histidine-tagged recombinant N-terminal fragment of type-1 mouse liver diacylglycerol acyltransferase (DGAT; EC 2.3.1.20), MmDGAT1(1-95)His6, was expressed in Escherichia coli, and used to investigate possible acyl-CoA-binding properties. Analysis of the purified fragment by MALDI-TOF mass spectrometry revealed a polypeptide with molecular mass of about 11 kDa which was consistent with the calculated molecular mass based on the deduced amino acid sequence. Lipidex-1000 binding assays indicated that MmDGAT1(1-95)His(6) interacted with long chain fatty acyl-CoAs similar to observations on DGAT1 from oilseed rape (Brassica napus). Binding, as a function of acyl-CoA concentration, differed for palmitoyl (16:0), stearoyl (18:0), and erucoyl (cisDelta(13)22:1)-CoA. Binding of stearoyl- or erucoyl-CoA to MmDGAT1(1-95)His(6) as a function of acyl-CoA concentration, however, was sigmoid and displayed positive cooperativity suggesting that MmDGAT1 may be subject to allosteric modulation by acyl-CoAs. An intra-polypeptide segment within the N-terminal region of MmDGAT1 contained remnants of an acyl-CoA-binding signature initially identified in plant DGAT1. The acyl-CoA-binding site in mammalian DGAT1 could represent a potential target for therapeutic interventions for disorders such as type-2 diabetes and obesity. | lld:pubmed |
| pubmed-article:18571500 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18571500 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18571500 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18571500 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18571500 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18571500 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18571500 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18571500 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:18571500 | pubmed:issn | 1090-2104 | lld:pubmed |
| pubmed-article:18571500 | pubmed:author | pubmed-author:LarocheAndréA | lld:pubmed |
| pubmed-article:18571500 | pubmed:author | pubmed-author:WeselakeRanda... | lld:pubmed |
| pubmed-article:18571500 | pubmed:author | pubmed-author:BurtonTracy... | lld:pubmed |
| pubmed-article:18571500 | pubmed:author | pubmed-author:WiehlerWillia... | lld:pubmed |
| pubmed-article:18571500 | pubmed:author | pubmed-author:SilotoRodrigo... | lld:pubmed |
| pubmed-article:18571500 | pubmed:author | pubmed-author:MadhavjiMilan... | lld:pubmed |
| pubmed-article:18571500 | pubmed:author | pubmed-author:BooraParveen... | lld:pubmed |
| pubmed-article:18571500 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18571500 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:18571500 | pubmed:volume | 373 | lld:pubmed |
| pubmed-article:18571500 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18571500 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18571500 | pubmed:pagination | 350-4 | lld:pubmed |
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| pubmed-article:18571500 | pubmed:meshHeading | pubmed-meshheading:18571500... | lld:pubmed |
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| pubmed-article:18571500 | pubmed:meshHeading | pubmed-meshheading:18571500... | lld:pubmed |
| pubmed-article:18571500 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18571500 | pubmed:articleTitle | An N-terminal fragment of mouse DGAT1 binds different acyl-CoAs with varying affinity. | lld:pubmed |
| pubmed-article:18571500 | pubmed:affiliation | Department of Agricultural, Food and Nutritional Science, 4-10 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alta., Canada T6G 2P5. | lld:pubmed |
| pubmed-article:18571500 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18571500 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:13350 | entrezgene:pubmed | pubmed-article:18571500 | lld:entrezgene |
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