Function
Peroxiredoxin (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid hyper oxide forming a Cys-SOH intermediate. A second Cys residue resolves the intermediate to a protein disulfide bond. The Prxs are divided into 3 types according to their intermediate resolving mechanism: typical 2-Cysteine Prx in which the Cys-Cys bond is formed between two subunits, atypical 2-Cys Prx in which the bond is formed within one subunit and 1-Cysteine Prx which uses a single Cys residue for the catalysis. Prx Q is the plant homolog of Bacterioferritin comigratory protein.
Typical 2-Cys Prx
- Prx 1 interacts with signaling molecules[1].
- Prx 2 is essential for sustaining erythrocyte life span[2].
- Prx 3 is mitochondria-specific.[3].
- Prx 4 localizes to the cytoplasm and regulates the activation of NF-κB[4].
Atypical 2-Cys Prx
- Prx 5 protects from mitochondrial DNA damage induced by H2O2[5].
1-Cys Prx
- Prx 6 reduces peroxidized membrane phospholipids[6].
Relevance
Prx are over expressed in cancer tissue[7]. Prx 4 mediates osteoclast activation in cancer cells[8].
Structural highlights
In the typical 2-cysteine Prx the [9]. . Water molecules is shown as red sphere.
3D Structures of Peroxiredoxin
Peroxiredoxin 3D structures
