Regulation of thioredoxin peroxidase activity by C-terminal truncation
Regulation of thioredoxin peroxidase activity by C-terminal truncation
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DOI：
10.1006/abbi.2001.2700
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发表时间：
2002-01-15
影响因子：
3.9
通讯作者：
Chae, HZ
中科院分区：
文献类型：
--
作者：
Koo, KH;Lee, S;Chae, HZ
硫氧还蛋白过氧化物酶是过氧还蛋白 (Prx) 家族的成员，它使用硫氧还蛋白 (Trx) 作为直接电子供体来还原过氧化物。我们从裂殖酵母中鉴定出 C 端截短的 TPx，并且还发现截短形式比完整形式更能抵抗 H2O2 的失活。对一系列重组 C 端截短突变体（Delta192、Delta191、Delta188、Delta184、Delta176 和 Delta165）的过氧化物酶测定表明，TPx 可以通过 C 端的连续截短而失活（Delta192）、重新激活 Delta191-Delta176）和重新激活（Delta165）。我们没有发现重新激活形式之间存在任何显着的动力学差异；然而，与完整形式相比，对 H2O2 (K-m = 5 muM) 的亲和力明显丧失（
Thioredoxin peroxidase is a member of peroxiredoxin (Prx) family, which uses a thioredoxin (Trx) as an immediate electron donor for the reduction of peroxide. We have identified C-terminal truncated TPx from Schizosaccharomyces pombe and also have found the truncated form is significantly tenacious against the inactivation of H2O2 than the intact form. Peroxidase assay of a series of recombinant C-terminal truncation mutants (Delta192, Delta191, Delta188, Delta184, Delta176, and Delta165) revealed that TPx could be inactivated (Delta192), reactivated Delta191-Delta176) and reinactivated (Delta165) by serial truncation from C-terminus. We did not find any significant kinetic difference among reactivated forms; however, distinctive loss of affinity to H2O2 (K-m = 5 muM) than that of the intact form (