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| pubmed-article:10419495 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:10419495 | pubmed:issue | 31 | lld:pubmed |
| pubmed-article:10419495 | pubmed:dateCreated | 1999-8-19 | lld:pubmed |
| pubmed-article:10419495 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10419495 | pubmed:abstractText | We report here the identification and characterization of human and mouse PECI, a novel gene that encodes a monofunctional peroxisomal Delta(3),Delta(2)-enoyl-CoA isomerase. Human and mouse PECI were identified on the basis of their sequence similarity to Eci1p, a recently characterized peroxisomal Delta(3),Delta(2)-enoyl-CoA isomerase from the yeast Saccharomyces cerevisiae. Cloning and sequencing of the human PECI cDNA revealed the presence of a 1077-base pair open reading frame predicted to encode a 359-amino acid protein with a mass of 39.6 kDa. The corresponding mouse cDNA contains a 1074-base pair open reading frame that encodes a 358-amino acid-long protein with a deduced mass of 39.4 kDa. Northern blot analysis demonstrated human PECI mRNA is expressed in all tissues. A bacterially expressed form of human PECI catalyzed the isomerization of 3-cis-octenoyl-CoA to 2-trans-octenoyl-CoA with a specific activity of 27 units/mg of protein. The human and mouse PECI proteins contain type-1 peroxisomal targeting signals, and human PECI was localized to peroxisomes by both subcellular fractionation and immunofluorescence microscopy techniques. The potential roles for this monofunctional Delta(3),Delta(2)-enoyl-CoA isomerase in peroxisomal metabolism are discussed. | lld:pubmed |
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| pubmed-article:10419495 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10419495 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10419495 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10419495 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10419495 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10419495 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10419495 | pubmed:author | pubmed-author:SchulzHH | lld:pubmed |
| pubmed-article:10419495 | pubmed:author | pubmed-author:GouldS JSJ | lld:pubmed |
| pubmed-article:10419495 | pubmed:author | pubmed-author:ZhangDD | lld:pubmed |
| pubmed-article:10419495 | pubmed:author | pubmed-author:GeisbrechtB... | lld:pubmed |
| pubmed-article:10419495 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10419495 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:10419495 | pubmed:volume | 274 | lld:pubmed |
| pubmed-article:10419495 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10419495 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10419495 | pubmed:pagination | 21797-803 | lld:pubmed |
| pubmed-article:10419495 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10419495 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10419495 | pubmed:articleTitle | Characterization of PECI, a novel monofunctional Delta(3), Delta(2)-enoyl-CoA isomerase of mammalian peroxisomes. | lld:pubmed |
| pubmed-article:10419495 | pubmed:affiliation | Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. | lld:pubmed |
| pubmed-article:10419495 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10419495 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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