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1.8.98.2: sulfiredoxin

This is an abbreviated version!
For detailed information about sulfiredoxin, go to the full flat file.

Word Map on EC 1.8.98.2

Reaction

peroxiredoxin-(S-hydroxy-S-oxocysteine)
+
ATP
 + 2 R-SH =
peroxiredoxin-(S-hydroxycysteine)
 +
ADP
 +
phosphate
 +
R-S-S-R

Synonyms

AtSrx, cysteine-sulfinic acid reductase, neoplastic progression 3, peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase, protein cysteine sulfinic acid reductase, Srx, Srx1, Srxn1, sulfiredoxin, sulfiredoxin 1, sulfiredoxin-1, sulphiredoxin

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.98 With other, known, physiological acceptors
                1.8.98.2 sulfiredoxin

Systematic Name

Systematic Name on EC 1.8.98.2 - sulfiredoxin

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SYSTEMATIC NAME
IUBMB Comments
peroxiredoxin-(S-hydroxy-S-oxocysteine):thiol oxidoreductase [ATP-hydrolysing; peroxiredoxin-(S-hydroxycysteine)-forming]
In the course of the reaction of EC 1.11.1.15, peroxiredoxin, its cysteine residue is alternately oxidized to the sulfenic acid, S-hydroxycysteine, and reduced back to cysteine. Occasionally the S-hydroxycysteine residue is further oxidized to the sulfinic acid S-hydroxy-S-oxocysteine, thereby inactivating the enzyme. The reductase provides a mechanism for regenerating the active form of peroxiredoxin, i.e. the peroxiredoxin-(S-hydroxycysteine) form. Apparently the reductase first catalyses the phosphorylation of the -S(O)-OH group by ATP to give -S(O)-O-P, which is attached to the peroxiredoxin by a cysteine residue, forming an -S(O)-S- link between the two enzymes. Attack by a thiol splits this bond, leaving the peroxiredoxin as the sulfenic acid and the reductase as the thiol.