IntEnz

EC 1.11.1.9 - Glutathione peroxidase

IntEnz Enzyme Nomenclature
EC 1.11.1.9

Names

Reaction

• 16833 [IUBMB]
  2

  glutathione

  glutathione

  Name origin: UniProt - CHECKED (C)

  CHEBI:57925

  Formula: C10H16N3O6S
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  H₂O₂

  H2O2

  Name origin: UniProt - CHECKED (C)

  CHEBI:16240

  Formula: H2O2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  glutathione disulfide

  glutathione disulfide

  Name origin: UniProt - CHECKED (C)

  CHEBI:58297

  Formula: C20H30N6O12S2
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

  +

  2

  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

Cofactor

• Se(2+)

Comments:

A protein containing a selenocysteine residue. Steroid and lipid hydroperoxides, but not the product of reaction of EC 1.13.11.12 lipoxygenase on phospholipids, can act as acceptor, but more slowly than H₂O₂ (cf. EC 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase).

Links to other databases

References

1. Chaudiere, J. and Tappel, A.L.
   Purification and characterization of selenium-glutathione peroxidase from hamster liver.
   Arch. Biochem. Biophys. 226: 448-457 (1983). [PMID: 6227287]
2. Grossmann, A. and Wendel, A.
   Non-reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids.
   Eur. J. Biochem. 135: 549-552 (1983). [PMID: 6413205]
3. Nakamura, W., Hosoda, S. and Hayashi, K.
   Purification and properties of rat liver glutathione peroxidase.
   Biochim. Biophys. Acta 358: 251-261 (1974).

[EC 1.11.1.9 created 1965, modified 1989]