Ontology highlight
ABSTRACT:
SUBMITTER: Sun CC
PROVIDER: S-EPMC4528153 | biostudies-literature | 2015 Aug
REPOSITORIES: biostudies-literature
Sun Cen-Cen CC Dong Wei-Ren WR Zhao Jing J Nie Li L Xiang Li-Xin LX Zhu Guan G Shao Jian-Zhong JZ
The Journal of biological chemistry 20150618 32
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 ...[more]