Probing the mechanism of a cyanobacterial Δ9 fatty acid desaturase from Spirulina platensis C1 (Arthrospira sp. PCC 9438)

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DOIResolve DOI: http://doi.org/10.1016/S1096-4959(01)00394-3
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TypeArticle
Journal titleComparative Biochemistry and Physiology Part B: Biochemistry & Molecular Biology
Volume129
Issue4
Pages831835; # of pages: 5
AbstractThe initial and rate determining step in the mechanism of fatty acid desaturases has been proposed to be breakage of one of the CH bonds at the site of the incipient double bond. This has been investigated and supported for a number of eukaryotic fatty acid desaturases through the use of kinetic isotope effect experiments with deuterated substrates. In order to probe the reaction catalyzed by the cyanobacterial Δ9 desaturase and compare it to the eukaryotic desaturases, the desC gene of Spirulina platensis, strain C1 (Arthrospira sp. PCC 9438) was expressed in a desaturase mutant of baker's yeast. Kinetic isotope effects were performed by culturing yeast transformants with deuterated thia-substituted stearic acids. A large kinetic isotope effect was found for the 9 position, in qualitative agreement with results from eukaryotic desaturases.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Plant Biotechnology Institute
Peer reviewedNo
NPARC number13053683
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Record identifierd74745fa-468e-476c-a8bf-78f2739a2ecc
Record created2009-11-25
Record modified2016-05-09
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