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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1996-10-11
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pubmed:databankReference |
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pubmed:abstractText |
beta-Ketoacyl-coenzyme A (CoA) synthase (KCS) catalyzes the condensation of malonyl-CoA with long-chain acyl-CoA. This reaction is the initial step of the microsomal fatty acyl-CoA elongation pathway responsible for formation of very long chain fatty acids (VLCFAs, or fatty acids with chain lengths > 18 carbons). Manipulation of this pathway is significant for agriculture, because it is the basis of conversion of high erucic acid rapeseed into canola. High erucic acid rapeseed oil, used as an industrial feedstock, is rich in VLCFAs, whereas the edible oil extracted from canola is essentially devoid of VLCFAs. Here, we report the cloning of a cDNA from developing jojoba embryos involved in microsomal fatty acid elongation. The jojoba cDNA is homologous to the recently cloned Arabidopsis FATTY ACID ELONGATION1 (FAE1) gene that has been suggested to encode KCS. We characterize the jojoba enzyme and present biochemical data indicating that the jojoba cDNA does indeed encode KCS. Transformation of low erucic acid rapeseed with the jojoba cDNA restored KCS activity to developing embryos and altered the transgenic seed oil composition to contain high levels of VLCFAs. The data reveal the key role KCS plays in determining the chain lengths of fatty acids found in seed oils.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-1600168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-16593964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-1892854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-1966276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-2029543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-2034657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-2051161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-2120038,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-2197415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-2231712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-2828858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-37916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-3954036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-6198133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-6279684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-6427224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-7002930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-7092205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-7704669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-7734965,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-8489015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-8539298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-8552723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8742713-942051
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1040-4651
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
281-92
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pubmed:dateRevised |
2010-9-10
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pubmed:meshHeading |
pubmed-meshheading:8742713-3-Oxoacyl-(Acyl-Carrier-Protein) Synthase,
pubmed-meshheading:8742713-Amino Acid Sequence,
pubmed-meshheading:8742713-Base Sequence,
pubmed-meshheading:8742713-Chromatography, Gel,
pubmed-meshheading:8742713-Cloning, Molecular,
pubmed-meshheading:8742713-DNA, Complementary,
pubmed-meshheading:8742713-DNA Primers,
pubmed-meshheading:8742713-Fatty Acids,
pubmed-meshheading:8742713-Microsomes,
pubmed-meshheading:8742713-Molecular Sequence Data,
pubmed-meshheading:8742713-Mutagenesis,
pubmed-meshheading:8742713-Oils,
pubmed-meshheading:8742713-Plants,
pubmed-meshheading:8742713-Plants, Genetically Modified,
pubmed-meshheading:8742713-Polymerase Chain Reaction,
pubmed-meshheading:8742713-Recombinant Proteins,
pubmed-meshheading:8742713-Seeds,
pubmed-meshheading:8742713-Sequence Homology, Amino Acid,
pubmed-meshheading:8742713-Substrate Specificity
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pubmed:year |
1996
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pubmed:articleTitle |
A jojoba beta-Ketoacyl-CoA synthase cDNA complements the canola fatty acid elongation mutation in transgenic plants.
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pubmed:affiliation |
Calgene, Inc., Davis, California 95616, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study
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