| DOI | Resolve DOI: https://doi.org/10.1016/S1096-4959(01)00394-3 |
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| Author | Search for: Meesapyodsuk, Dauenpen1; Search for: Reed, Darwin W.1; Search for: Cheevadhanarak, Supapon; Search for: Deshnium, Patcharaporn; Search for: Covello, Patrick S. |
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| Affiliation | - National Research Council of Canada. NRC Plant Biotechnology Institute
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| Format | Text, Article |
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| Abstract | The initial and rate determining step in the mechanism of fatty acid desaturases has been proposed to be breakage of one of the CH 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. |
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| Publication date | 2001 |
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| In | |
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| Language | English |
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| NPARC number | 13053683 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | d74745fa-468e-476c-a8bf-78f2739a2ecc |
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| Record created | 2009-11-25 |
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| Record modified | 2020-03-27 |
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