Article (Scientific journals)
Structural features conferring dual Geranyl/Farnesyl diphosphate synthase activity to an aphid prenyltransferase
Vandermoten, Sophie; Santini, Sébastien; Haubruge, Eric et al.
2009In Insect Biochemistry and Molecular Biology, 39 (10), p. 707-716
Peer Reviewed verified by ORBi
 

Files


Full Text
IB2065.pdf
Publisher postprint (1.03 MB)
I have transferred the copyright for this publication to the publisher
Request a copy
Full Text Parts
IBMB2009_Vandermoten.pdf
Author preprint (176.14 kB)
Download

All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
Aphid; Isoprenyl diphosphate synthase; Pheromone and juvenile hormone biosynthesis; Homology modelling; Molecular dynamics
Abstract :
[en] In addition to providing lipid chains for protein prenylation, short-chain isoprenyl diphosphate synthases (scIPPSs) play a pivotal role in the biosynthesis of numerous mevalonate pathway end-products, including insect juvenile hormone and terpenoid pheromones. For this reason, they are being considered as targets for pesticide development. Recently, we characterized an aphid scIPPS displaying dual geranyl diphosphate (GPP; C10)/farnesyl diphosphate (FPP; C15) synthase activity in vitro. To identify the mechanism(s) responsible for this dual activity, we assessed the product selectivity of aphid scIPPSs bearing mutations at Gln107 and/or Leu110, the fourth and first residue upstream from the “first aspartate-rich motif” (FARM), respectively. All but one resulted in significant changes in product chain-length selectivity, effectively increasing the production of either GPP (Q107E, L110W) or FPP (Q107F, Q107F–L110A); the other mutation (L110A) abolished activity. Although some of these effects could be attributed to changes in steric hindrance within the catalytic cavity, molecular dynamics simulations identified other contributing factors, including residue-ligand Van der Waals interactions and the formation of hydrogen bonds or salt bridges between Gln107 and other residues across the catalytic cavity, which constitutes a novel product chain-length determination mechanism for scIPPSs. Thus the aphid enzyme apparently evolved to maintain the capacity to produce both GPP and FPP through a balance between these mechanisms.
Disciplines :
Entomology & pest control
Author, co-author :
Vandermoten, Sophie ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech
Santini, Sébastien
Haubruge, Eric  ;  Université de Liège - ULiège > Services administratifs généraux > Vice-Recteur de Gembloux Agro Bio Tech - Gembloux Agro-Bio Tech
Heuze, Fabien;  Université de Liège - ULiège > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech
Francis, Frédéric  ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech
Brasseur, Robert ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech
Cusson, Michel
Charloteaux, Benoît ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech
Language :
English
Title :
Structural features conferring dual Geranyl/Farnesyl diphosphate synthase activity to an aphid prenyltransferase
Publication date :
October 2009
Journal title :
Insect Biochemistry and Molecular Biology
ISSN :
0965-1748
eISSN :
1879-0240
Publisher :
Pergamon Press (part of Elsevier Science), Oxford, United Kingdom
Volume :
39
Issue :
10
Pages :
707-716
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 12 November 2009

Statistics


Number of views
195 (37 by ULiège)
Number of downloads
142 (12 by ULiège)

Scopus citations®
 
30
Scopus citations®
without self-citations
24
OpenCitations
 
24

Bibliography


Similar publications



Contact ORBi