EC |
1.11.1.9 |
Accepted name: |
glutathione peroxidase |
Reaction: |
2 glutathione + H2O2 = glutathione disulfide + 2 H2O |
Other name(s): |
GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase |
Systematic name: |
glutathione:hydrogen-peroxide oxidoreductase |
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: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-66-5 |
References: |
1. |
Chaudiere, J. and Tappel, A.L. Purification and characterization of selenium-glutathione peroxidase from hamster liver. Arch. Biochem. Biophys. 226 (1983) 448–457. [DOI] [PMID: 6227287] |
2. |
Grossmann, A. and Wendel, A. Non-reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids. Eur. J. Biochem. 135 (1983) 549–552. [DOI] [PMID: 6413205] |
3. |
Nakamura, W., Hosoda, S. and Hayashi, K. Purification and properties of rat liver glutathione peroxidase. Biochim. Biophys. Acta 358 (1974) 251–261. |
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[EC 1.11.1.9 created 1965, modified 1989] |
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