http://purl.uniprot.org/citations/16982622 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16982622 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16982622 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
http://purl.uniprot.org/citations/16982622 | http://www.w3.org/2000/01/rdf-schema#comment | "A gene, named AtECH2, has been identified in Arabidopsis thaliana to encode a monofunctional peroxisomal enoyl-CoA hydratase 2. Homologues of AtECH2 are present in several angiosperms belonging to the Monocotyledon and Dicotyledon classes, as well as in a gymnosperm. In vitro enzyme assays demonstrated that AtECH2 catalyzed the reversible conversion of 2E-enoyl-CoA to 3R-hydroxyacyl-CoA. AtECH2 was also demonstrated to have enoyl-CoA hydratase 2 activity in an in vivo assay relying on the synthesis of polyhydroxyalkanoate from the polymerization of 3R-hydroxyacyl-CoA in the peroxisomes of Saccharomyces cerevisiae. AtECH2 contained a peroxisome targeting signal at the C-terminal end, was addressed to the peroxisome in S. cerevisiae, and a fusion protein between AtECH2 and a fluorescent protein was targeted to peroxisomes in onion cells. AtECH2 gene expression was strongest in tissues with high beta-oxidation activity, such as germinating seedlings and senescing leaves. The contribution of AtECH2 to the degradation of unsaturated fatty acids was assessed by analyzing the carbon flux through the beta-oxidation cycle in plants that synthesize peroxisomal polyhydroxyalkanoate and that were over- or underexpressing the AtECH2 gene. These studies revealed that AtECH2 participates in vivo to the conversion of the intermediate 3R-hydroxyacyl-CoA, generated by the metabolism of fatty acids with a cis (Z)-unsaturated bond on an even-numbered carbon, to the 2E-enoyl-CoA for further degradation through the core beta-oxidation cycle."xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m606383200"xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m606383200"xsd:string |
http://purl.uniprot.org/citations/16982622 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16982622 |
http://purl.uniprot.org/citations/16982622 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16982622 |
http://purl.uniprot.org/citations/16982622 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16982622 |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/author | "Poirier Y."xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/author | "Poirier Y."xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/author | "Hiltunen J.K."xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/author | "Hiltunen J.K."xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/author | "Goepfert S."xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/author | "Goepfert S."xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/pages | "35894-35903"xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/pages | "35894-35903"xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/title | "Identification and functional characterization of a monofunctional peroxisomal enoyl-CoA hydratase 2 that participates in the degradation of even cis-unsaturated fatty acids in Arabidopsis thaliana."xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/title | "Identification and functional characterization of a monofunctional peroxisomal enoyl-CoA hydratase 2 that participates in the degradation of even cis-unsaturated fatty acids in Arabidopsis thaliana."xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/volume | "281"xsd:string |
http://purl.uniprot.org/citations/16982622 | http://purl.uniprot.org/core/volume | "281"xsd:string |