水稻蛋白二硫键异构酶家族成员在形成和还原二硫键方面的差异活性。
Differential activity of rice protein disulfide isomerase family members for disulfide bond formation and reduction.
机构信息
Department of Food and Applied Life Sciences, Yamagata University, 1-23 Wakaba-Machi, Tsuruoka, Yamagata 997-8555, Japan.
出版信息
FEBS Open Bio. 2014 Aug 1;4:730-4. doi: 10.1016/j.fob.2014.07.007. eCollection 2014.
Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1, PDIL1;4, and PDIL2;3) and found that PDIL1;1 exhibited the highest catalytic activity for both disulfide bond formation and disulfide bond reduction. The activity of PDIL1;1-catalyzed disulfide bond reduction, in which two redox-active sites were involved, was enhanced by increasing the glutathione concentration. These results suggest that PDIL1;1 plays primary roles in both disulfide bond formation and disulfide bond reduction, which allow for redox control of protein quality and packaging.
蛋白质二硫键异构酶（PDI）是一类广泛存在于所有真核生物中的巯基-二硫键氧化还原酶，是形成二硫键的主要催化剂。在这里，我们研究了三个水稻（Oryza sativa）PDI 家族成员（PDIL1;1、PDIL1;4 和 PDIL2;3），发现 PDIL1;1 对二硫键形成和二硫键还原均表现出最高的催化活性。涉及两个氧化还原活性位点的 PDIL1;1 催化的二硫键还原活性可通过增加谷胱甘肽浓度而增强。这些结果表明，PDIL1;1 在二硫键形成和二硫键还原中均发挥主要作用，从而实现对蛋白质质量和包装的氧化还原控制。
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