Cysteine-independent Catalase-like Activity of Vertebrate Peroxiredoxin 1 (Prx1)*
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Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins that are known as thioredoxin peroxidases. Here we report that Prx1 proteins from Tetraodon nigroviridis and humans also possess a previously unknown catalase-like activity that is independent of Cys residues and reductants but dependent on iron. We identified that the GVL motif was essential to the catalase (CAT)-like activity of Prx1 but not to the Cys-dependent thioredoxin peroxidase (POX) activity, and we generated mutants lacking POX and/or CAT activities for individually delineating their functional features. We discovered that the TnPrx1 POX and CAT activities possessed different kinetic features in reducing H2O2. The overexpression of wild-type TnPrx1 and mutants differentially regulated the intracellular levels of reactive oxygen species and p38 phosphorylation in HEK-293T cells treated with H2O2. These observations suggest that the dual antioxidant activities of Prx1 may be crucial for organisms to mediate intracellular redox homeostasis.
author list (cited authors)
Sun, C., Dong, W., Zhao, J., Nie, L. i., Xiang, L., Zhu, G., & Shao, J.
complete list of authors
Sun, Cen-Cen||Dong, Wei-Ren||Zhao, Jing||Nie, Li||Xiang, Li-Xin||Zhu, Guan||Shao, Jian-Zhong