Linked Life Data

18655062

Source:http://linkedlifedata.com/resource/pubmed/id/18655062

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2008-8-7
pubmed:abstractText
The biotransformation of linoleic acid (LA) into conjugated linoleic acid (CLA) by microorganisms is a potentially useful industrial process. In most cases, however, the identities of proteins involved and the details of enzymatic activity regulation are far from clear. Here we summarize available data on the reaction mechanisms of CLA-producing enzymes characterized until now, from Butyrivibrio fibrisolvens, Lactobacillus acidophilus, Ptilota filicina, and Propionibacterium acnes. A general feature of enzymatic LA isomerization is the protein-assisted abstraction of an aliphatic hydrogen atom from position C-11, while the role of flavin as cofactor for the double bond activation in CLA-producing enzymes is also discussed with regard to the recently published three-dimensional structure of an isomerase from P. acnes. Combined data from structural studies, isotopic labeling experiments, and sequence comparison suggest that at least two different prototypical active site geometries occur among polyunsaturated fatty acid (PUFA) double bond isomerases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1439-7633
pubmed:author
pubmed:issnType
Electronic
pubmed:day
11
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1867-72
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Biochemistry of PUFA double bond isomerases producing conjugated linoleic acid.
pubmed:affiliation
Georg August University, Albrecht von Haller Institute for Plant Sciences, Department of Plant Biochemistry, Justus-von-Liebig Weg 11, 37077 Göttingen, Germany.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't