ID   1.8.98.2
DE   sulfiredoxin.
AN   peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase.
CA   [protein]-dithiol + ATP + S-hydroxy-S-oxy-L-cysteinyl-[peroxiredoxin] =
CA   [protein]-disulfide + ADP + phosphate + S-hydroxy-L-cysteinyl-
CA   [peroxiredoxin].
CC   -!- In the course of the reaction of EC 1.11.1.15, its cysteine residue
CC       is alternately oxidized to the sulfenic acid, S-hydroxycysteine,
CC       and reduced back to cysteine.
CC   -!- Occasionally the S-hydroxycysteine residue is further oxidized to the
CC       sulfinic acid S-hydroxy-S-oxocysteine, thereby inactivating the
CC       enzyme.
CC   -!- The reductase provides a mechanism for regenerating the active form
CC       of peroxiredoxin, i.e. the peroxiredoxin-(S-hydroxycysteine) form.
CC   -!- Apparently the reductase first catalyzes the phosphorylation of the
CC       -S(O)-OH group by ATP to give -S(O)-O-P, which is attached to the
CC       peroxiredoxin by a cysteine residue, forming an -S(O)-S- link between
CC       the two enzymes.
CC   -!- Attack by a thiol splits this bond, leaving the peroxiredoxin as the
CC       sulfenic acid and the reductase as the thiol.
DR   Q9URV9, SRX1_SCHPO ;  P36077, SRX1_YEAST ;  Q9BYN0, SRXN1_HUMAN;
DR   Q9D975, SRXN1_MOUSE;  Q8GY89, SRX_ARATH  ;  Q9VX10, SRX_DROME  ;
//