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Glutathione Reductase
Glutathione reductase, also known as GSR or GR (EC 1.8.1.7), belongs to the family of NADPH-dependent oxidoreductase and occurs in both prokaryotic and eukaryotic organisms. GR plays an essential central role in cell defense against reactive oxygen metabolites by efficiently maintaining the cellular reduced GSH pool through catalyzing the reduction of GSSG to GSH with the accompanying oxidation of NADPH. Glutathione reductase forms a flavin adenine dinucleotide (FAD)-bound homodimer. GR regulates GSH/GSSG ratio and supplies GSH for GPX and DHAR. The GPX and DHAR convert H2O2 and DHA into H2O and AsA, respectively. Although GR acquires the reduction power from NADPH, Hþ, it dissipates this power and, in turn, increases NADPþ/NADPH, Hþ ratio.
References
1.Gill SS, et al. Plant Physiol Biochem. 2013;70:204–212.
References
1.Gill SS, et al. Plant Physiol Biochem. 2013;70:204–212.
Others
Glutathione Reductase
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Glutathione
catalog no : M15692
cas no: 70-18-8
A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.
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L(-)-Glutathione
catalog no : M13826
cas no: 27025-41-8
A GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.