ID   1.11.1.27
DE   glutathione-dependent peroxiredoxin.
CA   a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide +
CA   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   -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so its
CC       regeneration involves direct interaction with a reductant molecule.
CC   -!- Glutathione-dependent peroxiredoxins have been reported from bacteria
CC       and animals, and appear to be 1-Cys enzymes.
CC   -!- The mechanism for the mammalian PRDX6 enzyme involves
CC       heterodimerization of the enzyme with pi-glutathione S-transferase,
CC       followed by glutathionylation of the oxidized cysteine residue.
CC   -!- Subsequent dissociation of the heterodimer yields glutathionylated
CC       peroxiredoxin, which is restored to the active form via spontaneous
CC       reduction by a second glutathione molecule.
CC   -!- Formerly EC 1.11.1.15.
DR   O77834, PRDX6_BOVIN;  Q5ZJF4, PRDX6_CHICK;  P30041, PRDX6_HUMAN;
DR   Q2PFL9, PRDX6_MACFA;  P86215, PRDX6_MESAU;  O08709, PRDX6_MOUSE;
DR   Q9TSX9, PRDX6_PIG  ;  Q5R7E0, PRDX6_PONAB;  O35244, PRDX6_RAT  ;
DR   P34227, PRX1_YEAST ;  P44758, PRX5_HAEIN ;  O69777, PRX5_RHIET ;
DR   Q53212, PRX5_SINFN ;  P73728, PRX5_SYNY3 ;
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