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Closed Access item Delta11 desaturases of Trichoplusia ni and Spodoptera littoralis catalytic behaviour
Gauthier, Lewis T.
Buist, Peter H.
|Keywords:||Desaturase, Hydroxylase, GC-MS, Spodoptera, Trichoplusia|
|Citation:||Insect Biochemistry and Molecular Biology 36(10): 822-825 (2006)|
|Abstract:||The Δ11 desaturases found in moths such as Spodoptera littoralis play a critical role in the biosynthesis of their sex pheromones. The ability to functionally express these enzymes in yeast has allowed one to study the transformation of long-chain fatty acyl substrates to their 11-ene products in greater mechanistic detail. In this article, we report on the detection and quantitation of a minor 11-hydroxylated byproduct (0.1% of total fatty acids), which is formed by the Δ11 desaturases found in Trichoplusia ni and Spodoptera littoralis. The position of the hydroxyl group was determined by characteristic mass spectral fragmentation of the trimethylsilyl derivatives and is in accord with predictions based on previous mechanistic investigations of the Spodoptera Δ11 desaturase. The level of 11-hydroxylation was insensitive to the mode of desaturase expression (constitutive vs. induced) and the presence or absence of a b5-fusion domain.|
Our findings suggest that in future, a search for hydroxylated products should be included in functional analyses of insect desaturase genes.
|Description:||4 pages, 1 table, 1 figure.-- PMID: 17027848 [PubMed].-- Printed version published Oct 2006.|
|Publisher version (URL):||http://dx.doi.org/10.1016/j.ibmb.2006.07.008|
|Appears in Collections:||(IQAC) Artículos|
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