过氧化氢
半胱氨酸
抗氧化剂
生物化学
化学
酶
细胞生物学
蛋白质超家族
活性氧
三磷酸腺苷
生物
基因
作者
Andrei V. Budanov,Anna Sablina,Elena Feinstein,Eugene V. Koonin,Peter M. Chumakov
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2004-04-23
卷期号:304 (5670): 596-600
被引量:683
标识
DOI:10.1126/science.1095569
摘要
Acting as a signal, hydrogen peroxide circumvents antioxidant defense by overoxidizing peroxiredoxins (Prxs), the enzymes that metabolize peroxides. We show that sestrins, a family of proteins whose expression is modulated by p53, are required for regeneration of Prxs containing Cys-SO 2 H, thus reestablishing the antioxidant firewall. Sestrins contain a predicted redox-active domain homologous to AhpD, the enzyme catalyzing the reduction of a bacterial Prx, AhpC. Purified Hi95 (sestrin 2) protein supports adenosine triphosphate–dependent reduction of overoxidized PrxI in vitro, indicating that unlike AhpD, which is a disulfide reductase, sestrins are cysteine sulfinyl reductases. As modulators of peroxide signaling and antioxidant defense, sestrins constitute potential therapeutic targets.
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