Source:http://linkedlifedata.com/resource/pubmed/id/10406955
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1999-8-26
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pubmed:abstractText |
The elongation of different substrates was studied using several subcellular fractions from Brassica napus rapeseed. In the presence of malonyl-CoA, NADH and NADPH, very-long-chain fatty acid (VLCFA) synthesis was observed from either oleoyl-CoA (acyl-CoA elongation) or endogenous primers (ATP-dependent elongation). No activity was detected using oleic acid as precursor. Acyl-CoA and ATP-dependent elongation activities were mainly associated with the 15 000 g/25 min membrane fraction. Reverse-phase TLC analysis showed that the proportions of fatty acids synthesized by these activities were different. Acyl-CoA elongation increased up to 60 microM oleoyl-CoA, and ATP-dependent elongation was maximum at 1 mM ATP. Both activities increased with malonyl-CoA concentration (up to 200 microM). Under all conditions tested, acyl-CoA elongation was higher than ATP-dependent elongation, and, in the presence of both ATP and oleoyl-CoA, the elongation activity was always lower. ATP strongly inhibited acyl-CoA elongation, whereas ATP-dependent elongation was slightly stimulated by low oleoyl-CoA concentrations (up to 15 microM) and decreased in the presence of higher concentrations. CoA (up to 150 microM) had no effect on the ATP-dependent elongation, whereas it inhibited the acyl-CoA elongation. These marked differences strongly support the presence in maturing rapeseed of two different elongating activities differently modulated by ATP and oleoyl-CoA.
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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/Acyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Erucic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Malonyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/erucic acid,
http://linkedlifedata.com/resource/pubmed/chemical/oleoyl-coenzyme A
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
263
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
464-70
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:10406955-Acyl Coenzyme A,
pubmed-meshheading:10406955-Adenosine Triphosphate,
pubmed-meshheading:10406955-Brassica,
pubmed-meshheading:10406955-Dose-Response Relationship, Drug,
pubmed-meshheading:10406955-Erucic Acids,
pubmed-meshheading:10406955-Fatty Acids,
pubmed-meshheading:10406955-Kinetics,
pubmed-meshheading:10406955-Malonyl Coenzyme A
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pubmed:year |
1999
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pubmed:articleTitle |
Evidence that oleoyl-CoA and ATP-dependent elongations coexist in rapeseed (Brassica napus L.).
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pubmed:affiliation |
Laboratoire de Biogenèse Membranaire, Université Victor Segalen Bordeaux 2, France Ecole Supérieure de Technologie des Biomolécules de Bordeaux (ESTBB), Université Victor Segalen Bordeaux 2, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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