Characterization of a novel aphid prenyltransferase displaying dual geranyl/farnesyl diphosphate synthase activity.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Vandermoten S,Charloteaux B,Santini S,Sen SE,Béliveau C,Vandenbol M,Francis F,Brasseur R,Cusson M,Haubruge E

doi

10.1016/j.febslet.2008.04.043

subject

Has Abstract

pub_date

2008-06-11 00:00:00

pages

1928-34

issue

13

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(08)00373-6

journal_volume

582

pub_type

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