Reconstitution of an apicoplast‐localised electron transfer pathway involved in the isoprenoid biosynthesis of <i>Plasmodium falciparum</i>

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<jats:p>In the malaria parasite <jats:italic>Plasmodium falciparum</jats:italic> isoprenoid precursors are synthesised inside a plastid‐like organelle (apicoplast) by the mevalonate independent 1‐deoxy‐<jats:sc>d</jats:sc>‐xylulose‐5‐phosphate (DOXP) pathway. The last reaction step of the DOXP pathway is catalysed by the LytB enzyme which contains a [4Fe–4S] cluster. In this study, LytB of <jats:italic>P. falciparum</jats:italic> was shown to be catalytically active in the presence of an NADPH dependent electron transfer system comprising ferredoxin and ferredoxin‐NADP<jats:sup>+</jats:sup> reductase. LytB and ferredoxin were found to form a stable protein complex. These data suggest that the ferredoxin/ferredoxin‐NADP<jats:sup>+</jats:sup> reductase redox system serves as the physiological electron donor for LytB in the apicoplast of <jats:italic>P. falciparum</jats:italic>.</jats:p>

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  • FEBS Letters

    FEBS Letters 579 (28), 6433-6438, 2005-11-02

    Wiley

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