Sulfiredoxin

In enzymology, a sulfiredoxin (EC 1.8.98.2) is an enzyme that catalyzes the chemical reaction

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

The 3 substrates of this enzyme are peroxiredoxin-(S-hydroxy-S-oxocysteine), ATP, and a thiol, whereas its 4 products are peroxiredoxin-(S-hydroxycysteine), ADP, phosphate, and a disulfide.

This enzyme is involved in antioxidant metabolism by re-activating peroxiredoxins, which are a group of peroxidases, when these enzymes are inhibited by over-oxidation.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with other, known, acceptors. The systematic name of this enzyme class is peroxiredoxin-(S-hydroxy-S-oxocysteine):thiol oxidoreductase . Other names in common use include Srx1, sulphiredoxin, and peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase.

Read more about Sulfiredoxin:  Function