peroxiredoxin-2; thioredoxin peroxidase 1; thioredoxin-dependent peroxide reductase 1; thiol-specific antioxidant protein; TSA; PRP; natural killer cell-enhancing factor B; NKEF-B (PRDX2 NKEFB TDPX1)
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Function
- role in redox regulation of the cell
- reduces peroxides with reducing equivalents provided through the thioredoxin system
- not able to receive electrons from glutaredoxin
- may play a role in eliminating peroxides generated during metabolism
- might participate in signaling cascades of growth factors & tumor necrosis factor-alpha by regulating intracellular H2O2
- interacts with TIPIN
- active site is redox-active Cys-51 oxidized to Cys-SOH
- Cys-SOH rapidly reacts Cys-172-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation
- the enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin
- inactivated upon oxidative stress by overoxidation of Cys-51 to Cys-SO2H & Cys-SO3H
- Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO2H may be irreversibly oxidized
2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH
Structure
- homodimer
- disulfide-linked, upon oxidation
- may be found as a toroid-shaped decamer composed of 5 dimers, depending on pH & Ca+2 concentration
- belongs to the ahpC/TSA family
- contains 1 thioredoxin domain
Compartment
More general terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/P32119.html
- ↑ NIEHS-SNPs http://egp.gs.washington.edu/data/prdx2/