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| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/11785945 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11785945 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11785945 | http://www.w3.org/2000/01/rdf-schema#comment | "Peroxisomes play an indispensable role in cellular fatty acid oxidation in higher eukaryotes by catalyzing the chain shortening of a distinct set of fatty acids and fatty acid derivatives including pristanic acid (2,6,10,14-tetramethylpentadecanoic acid). Earlier studies have shown that pristanic acid undergoes three cycles of beta-oxidation in peroxisomes to produce 4,8-dimethylnonanoyl-CoA (DMN-CoA) which is then transported to the mitochondria for full oxidation to CO(2) and H(2)O. In principle, this can be done via two different mechanisms in which DMN-CoA is either converted into the corresponding carnitine ester or hydrolyzed to 4,8-dimethylnonanoic acid plus CoASH. The latter pathway can only be operational if peroxisomes contain 4,8-dimethylnonanoyl-CoA thioesterase activity. In this paper we show that rat liver peroxisomes indeed contain 4,8-dimethylnonanoyl-CoA thioesterase activity. We have partially purified the enzyme involved from peroxisomes and identified the protein as the rat ortholog of a known human thioesterase using MALDI-TOF mass spectrometry in combination with the rat EST database. Heterologous expression studies in Escherichia coli established that the enzyme hydrolyzes not only DMN-CoA but also other branched-chain acyl-CoAs as well as straight-chain acyl-CoA-esters. Our data provide convincing evidence for the existence of the second pathway of acyl-CoA transport from peroxisomes to mitochondria by hydrolysis of the CoA-ester in peroxisomes followed by transport of the free acid to mitochondria, reactivation to its CoA-ester, and oxidation to CO(2) and H(2)O. (c)2002 Elsevier Science."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.org/dc/terms/identifier | "doi:10.1006/bbrc.2001.6245"xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.org/dc/terms/identifier | "doi:10.1006/bbrc.2001.6245"xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/author | "Ofman R."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/author | "Ofman R."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/author | "Wanders R.J."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/author | "Wanders R.J."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/author | "Dacremont G."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/author | "Dacremont G."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/author | "Spijer D."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/author | "Spijer D."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/author | "el Mrabet L."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/author | "el Mrabet L."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/pages | "629-634"xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/pages | "629-634"xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/title | "Demonstration of dimethylnonanoyl-CoA thioesterase activity in rat liver peroxisomes followed by purification and molecular cloning of the thioesterase involved."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/title | "Demonstration of dimethylnonanoyl-CoA thioesterase activity in rat liver peroxisomes followed by purification and molecular cloning of the thioesterase involved."xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/volume | "290"xsd:string |
| http://purl.uniprot.org/citations/11785945 | http://purl.uniprot.org/core/volume | "290"xsd:string |