PRDX4: Human peroxiredoxin 4 (thioredoxin peroxidase)
PDB Code: 2PN8
Oxidative stress is an inevitable process coupled to respiration and is defined as an imbalance between pro-oxidative and anti-oxidative states. This imbalance leads to an overall increase in cellular levels of reactive oxygen species such as hydrogen peroxide, superoxide anion or hydroxyl radicals that can progress to further lipid or macromolecule oxidation. Oxidative stress is accompanied with an altered gene transcription profile, carried out by redox-sensitive transcription factors, e.g., NFkB, AP1, or MAP kinases.
Various antioxidative mechanisms have been identified, such as small molecule antioxidants (glutathione, lipoic acid, ascorbic acid, tocopherol) or enzymatic mechanisms such as thioredoxin dependent peroxiredoxins (PRDXs) or glutathione dependent glutaredoxins (GLRXs). These enzymes regulate the intracellular redox state and inactivate hydrogen peroxide or lipid peroxides.
Peroxiredoxin 4 (Prdx4) belongs to a family of highly conserved peroxiredoxins, which have been identified in yeast, plant and animal cells, and most, if not all, eubacteria and archaea. Six members are expressed in mammalian cells (Prdx I to VI), which are classified into three subgroups based on the number and position of active site Cys residues that participate in catalysis. PRDX4 (Prx III) together with Prx 1, 2 and 3 belongs to the first subgroup.
The enzyme is widely expressed in human tissues with highest levels found in pancreas, liver, heart spleen and thymus. In sperm cells Prdx4 serves in the acrosome formation and vesicular reorganization during spermiogenesis.
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