ENZYME entry: EC 220.127.116.11
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|Peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH <=> peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R|
- In the course of the reaction of EC 18.104.22.168, 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
- The reductase provides a mechanism for regenerating the active form
of peroxiredoxin, i.e. the peroxiredoxin-(S-hydroxycysteine) form.
- Apparently the reductase first catalyzes 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.
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
entries corresponding to 1.8.98.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.8.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-