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 Lettjournal_title
FEBS lettersauthors
Vandermoten S,Charloteaux B,Santini S,Sen SE,Béliveau C,Vandenbol M,Francis F,Brasseur R,Cusson M,Haubruge Edoi
10.1016/j.febslet.2008.04.043subject
Has Abstractpub_date
2008-06-11 00:00:00pages
1928-34issue
13eissn
0014-5793issn
1873-3468pii
S0014-5793(08)00373-6journal_volume
582pub_type
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