Peroxiredoxin 6 (PRDX6)

1-Cys; AOP2; NSGPx; PRX; aiPLA2; p29; Acidic calcium-independent phospholipase A2; Antioxidant protein 2; Non-selenium glutathione peroxidase; Red blood cells page spot 12

Peroxiredoxin 6 (PRDX6)
Peroxiredoxin-6 is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell; it can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.
Kim et al. (1997) isolated a calcium-independent lysosomal PLA2 from a human myeloblast cell line. The predicted 224-amino acid protein contained the PLA2 catalytic motif, but no other significant homology to known phospholipases. Expressed protein had significant PLA2 activity on several substrates.

Organism species: Homo sapiens (Human)

Organism species: Mus musculus (Mouse)

Organism species: Rattus norvegicus (Rat)

Organism species: Bos taurus; Bovine (Cattle)