Open AccessProduction of recombinant 1‐deoxy‐ d ‐xylulose‐5‐phosphate synthase from Plasmodium vivax in Escherichia coli
Author(s) -
Handa Sumit,
Ramamoorthy Divya,
Spradling Tyler J.,
Guida Wayne C.,
Adams John H.,
Bendinskas Kestutis G.,
Merkler David J.
Publication year - 2013
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2013.01.007
Subject(s) - atp synthase , plasmodium vivax , plasmodium falciparum , biology , escherichia coli , biochemistry , malaria , enzyme , mevalonate pathway , plasmodium (life cycle) , biosynthesis , parasite hosting , gene , immunology , world wide web , computer science
Humanity is burdened by malaria as millions are infected with this disease. Although advancements have been made in the treatment of malaria, optimism regarding our fight against malaria must be tempered against the problem of drug resistance in the Plasmodium parasites causing malaria. New targets are required to overcome the resistance problem. The enzymes of the mevalonate‐independent pathway of isoprenoid biosynthesis are targets for the development of novel antimalarial drugs. One enzyme in this pathway, 1‐deoxy‐ d ‐xylulose‐5‐phosphate synthase (DXS), catalyzes the conversion of 1‐deoxy‐ d ‐xylulose‐5‐phosphate to isopentenylpyrophosphate and dimethylallyl phosphate. We demonstrate the use of a step deletion method to identify and eliminate the putative nuclear‐encoded and transit peptides from full length DXS to yield a truncated, active, and soluble form of Plasmodium vivax DXS, the DXS catalytic core (DXS cc ).