Overview on Peroxiredoxin

As in all biology, acronyms are overwhelming in Prx literature. A few of the more frequently used acronyms are TSA, AhpC, and TPx Prx was initially identified in yeast in 1987 and named thiol-specific antioxidant (TSA), because it was thought to remove reactive sulfur species (like RS , RSSR, or RSOOH) rather than reactive oxygen species (like O 2 , H 2 O 2 , or ROOH) Unlike enzymes known at the time to remove reactive oxygen species, purified TSA did not contain any redox cofactor such as a metal ion, heme, or flavin. Important clues to the actual enzymatic function of TSA were provided by database searches, which revealed a high sequence homology of TSA to AhpC (alkyl hydroperoxide reductase) identified in S. typhimurium in 1990 Subsequently, TSA was shown to reduce peroxides with thioredoxin (Trx) as the immediate hydrogen donor. Therefore the name of TSA was changed to thioredoxin peroxidase (TPx) in a manner analogous to glutathione peroxidase (GPx) (Chae et al., 1994a). It was then renamed Prx after realizing that certain members, for example 1-Cys Prxs, do not rely on Trx as the electron donor (Chae et al., 1994b). Proxiredoxin