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ENZYME

ENZYME entry: EC 1.11.1.25

Accepted Name
glutaredoxin-dependent peroxiredoxin
Reaction catalysed
[glutaredoxin]-dithiol + a hydroperoxide <=> [glutaredoxin]-disulfide + an alcohol + H2O
Comment(s)
  • Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins.
  • They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins .
  • The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine.
  • All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid).
  • The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes.
  • For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle.
  • In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond.
  • To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor.
  • The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule.
  • Glutaredoxin-dependent peroxiredoxins have been reported from bacteria, fungi, plants, and animals.
  • These enzymes are often able to use an alternative reductant such as thioredoxin or glutathione.
  • Formerly EC 1.11.1.15.
Cross-references
BRENDA1.11.1.25
EC2PDB1.11.1.25
ExplorEnz1.11.1.25
PRIAM enzyme-specific profiles1.11.1.25
KEGG Ligand Database for Enzyme Nomenclature1.11.1.25
IUBMB Enzyme Nomenclature1.11.1.25
IntEnz1.11.1.25
MEDLINEFind literature relating to 1.11.1.25
MetaCyc1.11.1.25
Rhea expert-curated reactions1.11.1.25
UniProtKB/Swiss-Prot
Q69TY4, PR2E1_ORYSJQ7F8S5, PR2E2_ORYSJP34227, PRX1_YEAST
Q7G959, PRX2A_ARATHQ9XEX2, PRX2B_ARATHQ9SRZ4, PRX2C_ARATH
Q9FR35, PRX2C_ORYSJO22711, PRX2D_ARATHQ949U7, PRX2E_ARATH
Q9M7T0, PRX2F_ARATHQ9SDD6, PRX2F_ORYSJA9PCL4, PRX2_POPTR

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