Cysteine-independent Catalase-like Activity of Vertebrate Peroxiredoxin 1 (Prx1). uri icon

abstract

  • 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.

published proceedings

  • J Biol Chem

altmetric score

  • 0.5

author list (cited authors)

  • Sun, C., Dong, W., Zhao, J., Nie, L. i., Xiang, L., Zhu, G., & Shao, J.

citation count

  • 3

complete list of authors

  • Sun, Cen-Cen||Dong, Wei-Ren||Zhao, Jing||Nie, Li||Xiang, Li-Xin||Zhu, Guan||Shao, Jian-Zhong

publication date

  • August 2015