Reconstitution of an apicoplast‐localised electron transfer pathway involved in the isoprenoid biosynthesis of <i>Plasmodium falciparum</i>
抄録
<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>
収録刊行物
-
- FEBS Letters
-
FEBS Letters 579 (28), 6433-6438, 2005-11-02
Wiley
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1364233270011599872
-
- NII論文ID
- 30002589144
-
- ISSN
- 18733468
- 00145793
-
- データソース種別
-
- Crossref
- CiNii Articles