| Title: | Delta11 desaturases of Trichoplusia ni and Spodoptera littoralis exhibit dual catalytic behaviour |
| Author(s): | Serra M; Gauthier LT; Fabrias G; Buist PH; |
| Address: | "Department of Biological Organic Chemistry, IIQAB-CSIC, Jordi Girona 18, 08034 Barcelona, Spain" |
| DOI: | 10.1016/j.ibmb.2006.07.008 |
| ISSN/ISBN: | 0965-1748 (Print) 0965-1748 (Linking) |
| Abstract: | "The Delta(11) 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 Delta(11) 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 Delta(11) 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" |
| Keywords: | "Animals Animals, Genetically Modified/metabolism Fatty Acid Desaturases/genetics/*metabolism Fatty Acids/chemistry/metabolism Hydroxylation Insect Proteins/genetics/*metabolism Mass Spectrometry Moths/*enzymology Recombinant Fusion Proteins/metabolism Sac;" |
| Notes: | "MedlineSerra, Montserrat Gauthier, Lewis T Fabrias, Gemma Buist, Peter H eng Research Support, Non-U.S. Gov't England 2006/10/10 Insect Biochem Mol Biol. 2006 Oct; 36(10):822-5. doi: 10.1016/j.ibmb.2006.07.008. Epub 2006 Aug 22" |
