PRDX1
Function
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (PubMed:9497357). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).
Post-translational modifications
Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity.
The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner.
Sequence Similarities
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Cellular localization
- Cytoplasm
- Melanosome
- Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Alternative names
PAGA, PAGB, TDPX2, PRDX1, Peroxiredoxin-1, Natural killer cell-enhancing factor A, Proliferation-associated gene protein, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2, Thioredoxin-dependent peroxiredoxin 1, NKEF-A, PAG