Née Guillaume, Zaffagnini Mirko, Trost Paolo, Issakidis-Bourguet Emmanuelle
Institut de Biotechnologie des Plantes, UMR 8618 CNRS/Université Paris-Sud, Orsay, France.
FEBS Lett. 2009 Sep 3;583(17):2827-32. doi: 10.1016/j.febslet.2009.07.035. Epub 2009 Jul 23.
Glucose-6-phosphate dehydrogenase (G6PDH) is the key enzyme of the oxidative pentose phosphate pathway supplying reducing power (as NADPH) in non-photosynthesizing cells. We have examined in detail the redox regulation of the plastidial isoform predominantly present in Arabidopsis green tissues (AtG6PDH1) and found that its oxidative activation is strictly dependent on plastidial thioredoxins (Trxs) that show differential efficiencies. Light/dark modulation of AtG6PDH1 was reproduced in vitro in a reconstituted ferredoxin/Trx system using f-type Trx allowing to propose a new function for this Trx isoform co-ordinating both reductive (Calvin cycle) and oxidative pentose phosphate pathways.
葡萄糖-6-磷酸脱氢酶（G6PDH）是氧化戊糖磷酸途径的关键酶，在非光合细胞中提供还原力（如NADPH）。我们详细研究了拟南芥绿色组织中主要存在的质体异构体（AtG6PDH1）的氧化还原调节，发现其氧化激活严格依赖于具有不同效率的质体硫氧还蛋白（Trxs）。在体外使用f型Trx的重组铁氧化还原蛋白/Trx系统中重现了AtG6PDH1的光/暗调节，从而为这种Trx异构体提出了一种新功能，即协调还原（卡尔文循环）和氧化戊糖磷酸途径。
