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ENZYME - 1.8.98.2 sulfiredoxin

Accepted Name
sulfiredoxin
Alternative Name(s)
peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase
Reaction catalysed
S-hydroxy-S-oxy-L-cysteinyl-[peroxiredoxin] + [protein]-dithiol + ATP = S-hydroxy-L-cysteinyl-[peroxiredoxin] + [protein]-disulfide + ADP + phosphate
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
Rhea expert-curated reactions1.8.98.2
UniProtKB/Swiss-Prot
Q9URV9, SRX1_SCHPOP36077, SRX1_YEASTQ9BYN0, SRXN1_HUMAN
Q9D975, SRXN1_MOUSEQ8GY89, SRX_ARATHQ9VX10, SRX_DROME

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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.-.-.-