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Description

Peroxiredoxin-1 (UniProt: Q06830, also known as EC:1.11.1.15, Natural killer cell-enhancing factor A, NKEF-A, Proliferation-associated gene protein, PAG, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2) is encoded by the PRDX1 (also known as PAGA, PAGB, TDPX2) gene (Gene ID: 5052 ) in human. Peroxiredoxins belong to a family of non-seleno peroxidases. Thus far six different mammalian isoforms have been reported and they all catalyze peroxide reduction of hydrogen peroxide, organic hydroperoxides and peroxynitrite. All peroxiredoxins share a conserved Cys residue that corresponds to the N-terminal Cys51 in mammalian peroxiredoxin-1. Peroxiredoxin 1-4 also contain an additional conserved Cys residue in the C-terminal region, Cys172. The N-terminal Cys51 is shown to be oxidized by hydrogen peroxide to form cysteine-sulfenic acid (Cys51-SOH) and reacts with Cys172-SH of the other subunit to produce an intermolecular disulfide, which can only be reduced by thioredoxin and not by glutathione or glutaredoxin. Peroxiredoxin-1 is constitutively expressed in most human cells and is induced to higher levels upon serum stimulation in cells. It is involved in redox regulation of the cell and important role in overcoming oxidative stress. Peroxiredoxin-1 also eliminates peroxides generated during drug metabolism. It is phosphorylated on Thr90 during the M-phase of cell cycle, which leads to over 80% reduction in its enzymatic activity.