Topological study of mechanistic diversity in conjugated fatty acid biosynthesis

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DOIResolve DOI: http://doi.org/10.1002/anie.201202080
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TypeArticle
Journal titleAngewandte Chemie International Edition
Volume51
Issue27
Pages66866690; # of pages: 5
SubjectC−H activation; desaturases; enzyme mechanisms; kinetic isotope effects; conformation analysis
AbstractVariations on an oxidative theme: The precision with which FAD2-type desaturases carry out C−H activation reactions on flexible lipidic substrates is astonishing. The conformational space available within the active site of these enzymes has been explored using deuterium-labeled substrates, and evidence for a novel quasi-eclipsed conformer has been uncovered. The scheme shows some prototypical substrate conformations.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Plant Biotechnology Institute
Peer reviewedNo
NRC number54667
NPARC number21186090
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Record identifierfa710324-f63e-4cc1-b7b6-f0391d33fdde
Record created2013-01-09
Record modified2016-05-09
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