Function
Prx3 operates through a redox cycle involving two critical cysteine residues: a peroxidatic cysteine (Cys47) and a resolving cysteine (Cys168). Cys47 reacts with peroxides, forming sulfenic acid, which then reacts with Cys168 to form an intersubunit disulfide bond within a dimer. This disulfide bond is subsequently reduced by the thioredoxin system. (thioredoxin and thioredoxin reductase), regenerating the enzyme for further catalysis. High levels of H₂O₂ can lead to overoxidation and inactivation of Cys47, a regulatory mechanism that acts as a sensor for oxidative stress.
To visualize the detailed steps of this process, click here for a scene showing the catalytic cycle of a typical 2-Cys peroxiredoxin. This scene should illustrate:
Disease
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Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.