Source:http://linkedlifedata.com/resource/pubmed/id/16982622
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
47
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pubmed:dateCreated |
2006-11-20
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon,
http://linkedlifedata.com/resource/pubmed/chemical/Enoyl-CoA Hydratase,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Unsaturated,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35894-903
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pubmed:meshHeading |
pubmed-meshheading:16982622-Amino Acid Sequence,
pubmed-meshheading:16982622-Arabidopsis,
pubmed-meshheading:16982622-Arabidopsis Proteins,
pubmed-meshheading:16982622-Carbon,
pubmed-meshheading:16982622-Catalysis,
pubmed-meshheading:16982622-Enoyl-CoA Hydratase,
pubmed-meshheading:16982622-Fatty Acids,
pubmed-meshheading:16982622-Fatty Acids, Unsaturated,
pubmed-meshheading:16982622-Molecular Sequence Data,
pubmed-meshheading:16982622-Onions,
pubmed-meshheading:16982622-Oxygen,
pubmed-meshheading:16982622-Peroxisomes,
pubmed-meshheading:16982622-Plant Proteins,
pubmed-meshheading:16982622-Recombinant Fusion Proteins,
pubmed-meshheading:16982622-Saccharomyces cerevisiae,
pubmed-meshheading:16982622-Sequence Homology, Amino Acid
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pubmed:year |
2006
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pubmed:articleTitle |
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.
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pubmed:affiliation |
Département de Biologie Moléculaire Végétale, Biophore Building, Université de Lausanne, CH-1015, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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