| EC |
1.11.1.17 |
| Accepted name: |
glutathione amide-dependent peroxidase |
| Reaction: |
2 glutathione amide + H2O2 = glutathione amide disulfide + 2 H2O |
| Systematic name: |
glutathione amide:hydrogen-peroxide oxidoreductase |
| Comments: |
This enzyme, which has been characterized from the proteobacterium Marichromatium gracile, is a chimeric protein, containing a peroxiredoxin-like N-terminus and a glutaredoxin-like C terminus. The enzyme has peroxidase activity towards hydrogen peroxide and several small alkyl hydroperoxides, and is thought to represent an early adaptation for fighting oxidative stress [1]. The glutathione amide disulfide produced by this enzyme can be restored to glutathione amide by EC 1.8.1.16 (glutathione amide reductase). |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Vergauwen, B., Pauwels, F., Jacquemotte, F., Meyer, T.E., Cusanovich, M.A., Bartsch, R.G. and Van Beeumen, J.J. Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J. Biol. Chem. 276 (2001) 20890–20897. [DOI] [PMID: 11399772] |
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| [EC 1.11.1.17 created 2010] |
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