Röhrich René C, Englert Nadine, Troschke Katrin, Reichenberg Armin, Hintz Martin, Seeber Frank, Balconi Emanuela, Aliverti Alessandro, Zanetti Giuliana, Köhler Uwe, Pfeiffer Matthias, Beck Ewald, Jomaa Hassan, Wiesner Jochen
Biochemisches Institut, Justus-Liebig-Universität Giessen, Friedrichstrasse 24, 35392 Giessen, Germany.
FEBS Lett. 2005 Nov 21;579(28):6433-8. doi: 10.1016/j.febslet.2005.10.037. Epub 2005 Nov 2.
In the malaria parasite Plasmodium falciparum isoprenoid precursors are synthesised inside a plastid-like organelle (apicoplast) by the mevalonate independent 1-deoxy-d-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 P. falciparum was shown to be catalytically active in the presence of an NADPH dependent electron transfer system comprising ferredoxin and ferredoxin-NADP(+) reductase. LytB and ferredoxin were found to form a stable protein complex. These data suggest that the ferredoxin/ferredoxin-NADP(+) reductase redox system serves as the physiological electron donor for LytB in the apicoplast of P. falciparum.
在疟原虫恶性疟原虫中，类异戊二烯前体是通过甲羟戊酸非依赖型的1-脱氧-D-木酮糖-5-磷酸（DOXP）途径在类质体样细胞器（顶质体）内合成的。DOXP途径的最后一个反应步骤由含有[4Fe-4S]簇的LytB酶催化。在本研究中，恶性疟原虫的LytB在包含铁氧还蛋白和铁氧还蛋白-NADP(+)还原酶的NADPH依赖型电子传递系统存在的情况下显示出催化活性。发现LytB和铁氧还蛋白形成稳定的蛋白质复合物。这些数据表明，铁氧还蛋白/铁氧还蛋白-NADP(+)还原酶氧化还原系统作为恶性疟原虫顶质体中LytB的生理电子供体。
