| EC |
1.8.1.16 |
| Accepted name: |
glutathione amide reductase |
| Reaction: |
2 glutathione amide + NAD+ = glutathione amide disulfide + NADH + H+ |
| Other name(s): |
GAR |
| Systematic name: |
glutathione amide:NAD+ oxidoreductase |
| Comments: |
A dimeric flavoprotein (FAD). The enzyme restores glutathione amide disulfide, which is produced during the reduction of peroxide by EC 1.11.1.17 (glutathione amide-dependent peroxidase), back to glutathione amide (it catalyses the reaction in the opposite direction to that shown). The enzyme belongs to the family of flavoprotein disulfide oxidoreductases, but unlike other members of the family, which are specific for NADPH, it prefers NADH [1]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| 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] |
| 2. |
Vergauwen, B., Van Petegem, F., Remaut, H., Pauwels, F. and Van Beeumen, J.J. Crystallization and preliminary X-ray crystallographic analysis of glutathione amide reductase from Chromatium gracile. Acta Crystallogr. D Biol. Crystallogr. 58 (2002) 339–340. [PMID: 11807270] |
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| [EC 1.8.1.16 created 2010] |
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