Home  |  Contact
Due to maintenance work, this service will be unavailable Mon Feb 13 between 07:00 and 09:30 - CET. Apologies for the inconvenience.

ENZYME entry: EC

Accepted Name
Alternative Name(s)
peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase.
Reaction catalysed
[protein]-dithiol + ATP + S-hydroxy-S-oxy-L-cysteinyl-[peroxiredoxin] <=> [protein]-disulfide + ADP + phosphate + S-hydroxy-L-cysteinyl-[peroxiredoxin]
  • In the course of the reaction of EC, 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 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 profiles1.8.98.2
KEGG Ligand Database for Enzyme Nomenclature1.8.98.2
IUBMB Enzyme Nomenclature1.8.98.2
MEDLINEFind literature relating to
Rhea expert-curated reactions1.8.98.2

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot 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.-.-.-