ORBi: Vandermoten Sophie - Characterization of a novel aphid prenyltransferase displaying dual geranyl/farnesyl diphosphate synthase activity

Reference : Characterization of a novel aphid prenyltransferase displaying dual geranyl/farnesyl dip...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Entomology & pest control
	To cite this reference:	http://hdl.handle.net/2268/18461

Title :	Characterization of a novel aphid prenyltransferase displaying dual geranyl/farnesyl diphosphate synthase activity
Language :	English
Author, co-author :	Vandermoten, Sophie [Université de Liège > > Gembloux Agro-Bio Tech >]
	Charloteaux, Benoît [Université de Liège > > Gembloux Agro-Bio Tech >]
	Santini, S. [> > > >]
	Sen, Se. [> > > >]
	Beliveau, C. [> > > >]
	Vandenbol, Micheline [Université de Liège > > Gembloux Agro-Bio Tech >]
	Francis, Frédéric [Université de Liège > > Gembloux Agro-Bio Tech >]
	Brasseur, Robert [Université de Liège > > Gembloux Agro-Bio Tech >]
	Cusson, M. [> > > >]
	Haubruge, Eric [Université de Liège > > Gembloux Agro-Bio Tech >]
Publication date :	2008
Journal title :	FEBS Letters
Volume :	582
Issue/season :	16
Pages :	1928–1934
Audience :	International
ISSN :	0014-5793
Keywords :	[en] Aphid ; Isoprenyl diphosphate synthase ; Geranyl diphosphate synthase ; Farnesyl diphosphate synthase ; Bifunctional enzyme ; Homology Modelling
Abstract :	[en] We report on the cDNA cloning and characterization of a novel short-chain isoprenyl diphosphate synthase from the aphid Myzus persicae. Of the three IPPS cDNAs we cloned, two yielded prenyltransferase activity following expression in Escherichia coli; these cDNAs encode identical proteins except for the presence, in one of them, of an N-terminal mitochondrial targeting peptide. Although the aphid enzyme was predicted to be a farnesyl diphosphate synthase by BLASTP analysis, rMpIPPS, when isopentenyl diphosphate and dimethylallyl diphosphate are supplied as substrates, typically generated geranyl diphosphate (C10) as its main product, along with significant quantities of farnesyl diphosphate (C15). Analysis of an MpIPPS homology model pointed to substitutions that could confer GPP/FPP synthase activity to the aphid enzyme.
Permalink :	http://hdl.handle.net/2268/18461
DOI :	10.1016/j.febslet.2008.06.002

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Open access	FEBSL2008_Vandermotenet al.pdf	I have transferred the copyright for this publication to the publisher	Author preprint	419.1 kB	View/Open
Restricted access	FEBS32565.pdf	I have transferred the copyright for this publication to the publisher	Publisher postprint	1.11 MB	Request copy

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