Source:http://linkedlifedata.com/resource/pubmed/id/16105701
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2005-12-7
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pubmed:abstractText |
The Delta5-desaturase from Bacillus subtilis has been cloned in Escherichia coli BL21 cells and its enzyme activity has been investigated as a function of temperature and oxygenation by analyzing methyl ester adducts from the total lipid extract in GC-MS measurements. The present data bring out that the activity of recombinant Delta5-desaturase, at 20-22 degrees C and 20% oxygen, is surprisingly high yielding 22% of C16:1,Delta5 (5-cis-palmitoleic acid) and 13% C18:2, Delta5 Delta11 (efedrenic acid). Lower amounts of other mono- and doubly-Delta5-unsaturated fatty acids were also detected. These findings demonstrate that Delta5-desaturase can accept a multiplicity of substrates and is endowed with an unprecedented activity among other acyl-lipid desaturases thus representing a unique tool for the production of rare Delta5 unsaturated fatty acid derivatives.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid Desaturases,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/delta-5 fatty acid desaturase
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0168-1656
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
121
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
49-53
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16105701-Bacillus subtilis,
pubmed-meshheading:16105701-Bacterial Proteins,
pubmed-meshheading:16105701-Escherichia coli,
pubmed-meshheading:16105701-Fatty Acid Desaturases,
pubmed-meshheading:16105701-Oxidation-Reduction,
pubmed-meshheading:16105701-Phospholipids,
pubmed-meshheading:16105701-Recombinant Proteins
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pubmed:year |
2006
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pubmed:articleTitle |
The desaturase from Bacillus subtilis, a promising tool for the selective olefination of phospholipids.
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pubmed:affiliation |
Department of Biochemical Sciences, University "La Sapienza", Piazza Aldo Moro 5, 00185 Rome, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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