Home  |  Contact

ENZYME entry: EC 1.8.98.2

Accepted Name
Sulfiredoxin.
Alternative Name(s)
Peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase.
Reaction catalysed
Peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH <=> peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
Comment(s)
  • In the course of the reaction of EC 1.11.1.15, 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.
Cross-references
BRENDA1.8.98.2
EC2PDB1.8.98.2
ExplorEnz1.8.98.2
PRIAM enzyme-specific profiles1.8.98.2
KEGG Ligand Database for Enzyme Nomenclature1.8.98.2
IUBMB Enzyme Nomenclature1.8.98.2
IntEnz1.8.98.2
MEDLINEFind literature relating to 1.8.98.2
MetaCyc1.8.98.2
UniProtKB/Swiss-Prot
Q9URV9, SRX1_SCHPO;  P36077, SRX1_YEAST;  Q9BYN0, SRXN1_HUMAN;  
Q9D975, SRXN1_MOUSE;  Q8GY89, SRX_ARATH;  Q9VX10, SRX_DROME;  

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.-.-.-