Document Detail


Delta11 desaturases of Trichoplusia ni and Spodoptera littoralis exhibit dual catalytic behaviour.
MedLine Citation:
PMID:  17027848     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Montserrat Serra; Lewis T Gauthier; Gemma Fabrias; Peter H Buist
Related Documents :
20187298 - Oxygen-induced expression of delta(6)-, delta(9)- and delta(12)-desaturase genes modula...
15898118 - Pheromone biosynthetic pathways in the moths heliothis subflexa and heliothis virescens.
2321968 - The delta 12-desaturase from the house cricket, acheta domesticus (orthoptera: gryllida...
2327968 - Pseudoarginine: synthesis and properties of derivatives of delta-(1-imidazolyl)norvaline.
7085638 - The exchange of fe3+ between acetohydroxamic acid and transferrin. spectrophotometric e...
3489278 - Duodenal output of lactoferrin in normal subjects and correlation to output of amylase,...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-08-22
Journal Detail:
Title:  Insect biochemistry and molecular biology     Volume:  36     ISSN:  0965-1748     ISO Abbreviation:  Insect Biochem. Mol. Biol.     Publication Date:  2006 Oct 
Date Detail:
Created Date:  2006-10-09     Completed Date:  2006-12-15     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9207282     Medline TA:  Insect Biochem Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  822-5     Citation Subset:  IM    
Affiliation:
Department of Biological Organic Chemistry, IIQAB-CSIC, Jordi Girona 18, 08034 Barcelona, Spain.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
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
Saccharomyces cerevisiae / genetics
Spodoptera / enzymology*
Chemical
Reg. No./Substance:
0/Fatty Acids; 0/Insect Proteins; 0/Recombinant Fusion Proteins; EC 1.14.19.-/Fatty Acid Desaturases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Active ammonia absorption in the midgut of the Tobacco hornworm Manduca sexta L.: transport studies ...
Next Document:  New flow cytometric technique for the evaluation of circulating endothelial progenitor cell levels i...