ID 1.11.1.25 DE glutaredoxin-dependent peroxiredoxin. CA [glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]-disulfide + CA an alcohol + H2O. CC -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant CC proteins. CC -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys CC and 1-Cys peroxiredoxins . CC -!- The peroxidase reaction comprises two steps centered around a redox- CC active cysteine called the peroxidatic cysteine. CC -!- All three peroxiredoxin classes have the first step in common, CC in which the peroxidatic cysteine attacks the peroxide substrate and CC is oxidized to S-hydroxycysteine (a sulfenic acid). CC -!- The second step of the peroxidase reaction, the regeneration of CC cysteine from S-hydroxycysteine, distinguishes the three CC peroxiredoxin classes. CC -!- For typical 2-Cys Prxs, in the second step, the peroxidatic CC S-hydroxycysteine from one subunit is attacked by the 'resolving' CC cysteine located in the C-terminus of the second subunit, to form an CC intersubunit disulfide bond, which is then reduced by one of several CC cell-specific thiol-containing reductants completing the catalytic CC cycle. CC -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its CC resolving cysteine are in the same polypeptide, so their reaction CC forms an intrachain disulfide bond. CC -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use CC thioredoxin as an electron donor. CC -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so its CC regeneration involves direct interaction with a reductant molecule. CC -!- Glutaredoxin-dependent peroxiredoxins have been reported from CC bacteria, fungi, plants, and animals. CC -!- These enzymes are often able to use an alternative reductant such as CC thioredoxin or glutathione. CC -!- Formerly EC 1.11.1.15. DR Q69TY4, PR2E1_ORYSJ; Q7F8S5, PR2E2_ORYSJ; P34227, PRX1_YEAST ; DR Q7G959, PRX2A_ARATH; Q9XEX2, PRX2B_ARATH; Q9SRZ4, PRX2C_ARATH; DR Q9FR35, PRX2C_ORYSJ; O22711, PRX2D_ARATH; Q949U7, PRX2E_ARATH; DR Q9M7T0, PRX2F_ARATH; Q9SDD6, PRX2F_ORYSJ; A9PCL4, PRX2_POPTR ; //