Source:http://linkedlifedata.com/resource/pubmed/id/10419495
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
31
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| pubmed:dateCreated |
1999-8-19
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| pubmed:databankReference | |
| 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.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
30
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| pubmed:volume |
274
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
21797-803
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:10419495-Amino Acid Sequence,
pubmed-meshheading:10419495-Animals,
pubmed-meshheading:10419495-Carbon-Carbon Double Bond Isomerases,
pubmed-meshheading:10419495-Carcinoma, Hepatocellular,
pubmed-meshheading:10419495-Cells, Cultured,
pubmed-meshheading:10419495-Cloning, Molecular,
pubmed-meshheading:10419495-Escherichia coli,
pubmed-meshheading:10419495-Fibroblasts,
pubmed-meshheading:10419495-Genes,
pubmed-meshheading:10419495-Humans,
pubmed-meshheading:10419495-Kinetics,
pubmed-meshheading:10419495-Liver Neoplasms,
pubmed-meshheading:10419495-Mammals,
pubmed-meshheading:10419495-Mice,
pubmed-meshheading:10419495-Microbodies,
pubmed-meshheading:10419495-Molecular Sequence Data,
pubmed-meshheading:10419495-Open Reading Frames,
pubmed-meshheading:10419495-Polymerase Chain Reaction,
pubmed-meshheading:10419495-Protein Biosynthesis,
pubmed-meshheading:10419495-Recombinant Proteins,
pubmed-meshheading:10419495-Saccharomyces cerevisiae,
pubmed-meshheading:10419495-Sequence Alignment,
pubmed-meshheading:10419495-Sequence Homology, Amino Acid,
pubmed-meshheading:10419495-Skin,
pubmed-meshheading:10419495-Tumor Cells, Cultured
|
| pubmed:year |
1999
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| pubmed:articleTitle |
Characterization of PECI, a novel monofunctional Delta(3), Delta(2)-enoyl-CoA isomerase of mammalian peroxisomes.
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| pubmed:affiliation |
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|