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 .
The expected taxonomic range for this enzyme is: Bacteria, Archaea
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SYSTEMATIC NAME
IUBMB Comments
glutathione amide:NAD+ oxidoreductase
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].
grown at 21°C by the hanging-drop vapour-diffusion method using lithium sulfate as a precipitant in the presence of nickel ions. The crystals belong to space group P4(1), with unit-cell parameters a = b = 71.93, c = 223.85 A, alpha = beta = gamma = 90° and one dimer per asymmetric unit. A full set of X-ray diffraction data is collected to 2.1 A resolution with a completeness of 95.2%
Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling
van Petegem, F.; de Vos, D.; Savvides, S.; Vergauwen, B.; van Beeumen, J.
Understanding nicotinamide dinucleotide cofactor and substrate specificity in class I flavoprotein disulfide oxidoreductases: crystallographic analysis of a glutathione amide reductase
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