Division of Life and Pharmaceutical Sciences, Ewha Womans University,Seoul 120-750, Korea.
J Biol Chem. 2012 Feb 10;287(7):4403-10. doi: 10.1074/jbc.R111.283432. Epub 2011 Dec 6.
Peroxiredoxins (Prxs) contain an active site cysteine that is sensitive to oxidation by H(2)O(2). Mammalian cells express six Prx isoforms that are localized to various cellular compartments. The oxidized active site cysteine of Prx can be reduced by a cellular thiol, thus enabling Prx to function as a locally constrained peroxidase. Regulation of Prx via phosphorylation in response to extracellular signals allows the local accumulation of H(2)O(2) and thereby enables its messenger function. The fact that the oxidation state of the active site cysteine of Prx can be transferred to other proteins that are less intrinsically susceptible to H(2)O(2) also allows Prx to function as an H(2)O(2) sensor.
过氧化物酶（Prx）含有一个活性位点半胱氨酸，容易被 H(2)O(2)氧化。哺乳动物细胞表达六种 Prx 同工型，定位于各种细胞区室。Prx 的氧化活性位点半胱氨酸可以被细胞内的巯基还原，从而使 Prx 能够作为局部受限的过氧化物酶发挥作用。Prx 通过对外界信号的磷酸化调节，可以局部积累 H(2)O(2)，从而发挥其信使功能。此外，Prx 的活性位点半胱氨酸的氧化状态可以转移到其他对 H(2)O(2 不太敏感的蛋白质上，这也使得 Prx 能够作为 H(2)O(2)传感器发挥作用。
