Peroxiredoxins (Prxs) are an unusual family of thiol-specific peroxidases that possess a binding site for H2O2 and rely on a conserved cysteine residue for rapid reaction with H2O2. Among 6 mammalian isoforms (Prx I to VI), Prx I and Prx II are mainly found in the cytosol and nucleus. Prx I and Prx II function as antioxidant enzymes and protein chaperone under oxidative distress conditions. Under oxidative eustress conditions, Prx I and Prx II regulate the levels of H2O2 at specific area of the cells as well as sense and transduce H2O2 signaling to target proteins. Prx I and Prx II are known to be covalently modified on multiple sites: Prx I is hyperoxidized on Cys52; phosphorylated on Ser32, Thr90, and Tyr194; acetylated on Lys7, Lys16, Lys27, Lys35, and Lys197; glutathionylated on Cys52, Cys83, and Cys173; and nitrosylated on Cys52 and Cys83, whereas Prx II is hyperoxidized on Cys51; phosphorylated on Thr89, Ser112, and Thr182; acetylated on Ala2 and Lys196; glutathionylated on Cys51 and Cys172; and nitrosylated on Cys51 and Cys172. In this review, we describe how these post-translational modifications affect various functions of Prx I and Prx II.

中文翻译：

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2-Cys过氧化物酶，I和II的多功能以及通过翻译后修饰的调控。

过氧化物酶（Prxs）是硫醇特异性过氧化物酶的不寻常家族，其具有与H2O2的结合位点，并且依赖于保守的半胱氨酸残基与H2O2快速反应。在6种哺乳动物同工型（Prx I至VI）中，Prx I和Prx II主要存在于细胞质和细胞核中。Prx I和Prx II在氧化窘迫条件下起抗氧化酶和蛋白伴侣的作用。在氧化性应激条件下，Prx I和Prx II调节细胞特定区域的H2O2水平，以及将H2O2信号传导并传导至目标蛋白。已知Prx I和Prx II在多个位点被共价修饰：Prx I在Cys52上被过度氧化；在Ser32，Thr90和Tyr194上磷酸化; 在Lys7，Lys16，Lys27，Lys35和Lys197上乙酰化；在Cys52，Cys83和Cys173上进行谷胱甘肽化；然后在Cys52和Cys83上亚硝化 而Prx II在Cys51上被过度氧化；在Thr89，Ser112和Thr182上磷酸化; 在Ala2和Lys196上乙酰化；在Cys51和Cys172上谷胱甘肽化；并在Cys51和Cys172上亚硝化。在这篇综述中，我们描述了这些翻译后修饰如何影响Prx I和Prx II的各种功能。