thioredoxin-dependent peroxide reductase, mitochondrial; peroxiredoxin-3; PRX III; antioxidant protein 1; AOP-1; protein MER5 homolog; HBC189 (PRDX3, AOP1)
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Function
- role in redox regulation of the cell
- protects radical-sensitive enzymes from oxidative damage by a radical-generating system
- acts synergistically with MAP3K13 to regulate activation of NF-kappa-B in the cytosol
- disulfide-linked, upon oxidation
- binds MAP3K13
- the active site is the redox-active Cys-108 oxidized to Cys-SOH
- Cys-SOH rapidly reacts with Cys-229-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
- irreversibly inactivated by overoxidation of Cys-108 (to Cys-SO(3)H) upon oxidative stress
Structure
- dodecameric ring assembled from homodimeric units
- the rings have an approximate diameter of 150 A & a central hole of 70 A. 3-5% of the rings are interlocked by pairs
- belongs to the ahpC/TSA family
- contains 1 thioredoxin domain
Compartment
More general terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/P30048.html
- ↑ NIEHS-SNPs http://egp.gs.washington.edu/data/prdx3/