Glutathione Reductase human

Research area: Cell signaling. Glutathione Reductase belongs to the homodimericFAD−disulfide oxidoreductases family. is made up of highly conserved domains such as two Rossmann fold domains, where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain. It favors its accumulation in the regions of high electron flux in cells where reactive species are generated.

Human glutathione reductase has been used in:

• glutathione reductase activity assay
• oxidative stress analysis
• redox assays

Human glutathione reductase is suitable as cytostatic and antimalarialagent. It may also be used to protect against malaria by mimicking favism by blockingthe enzyme with specific inhibitors.

Glutathione reductase enzyme is a homodimeric enzyme containing 1 FAD molecule and 1 NADPH binding domain per subunit. Both human GR (hGR) and Plasmodium falciparum GR (PfGR) are essential for the survival of the malaria parasite within the human erythrocyte. Thus, this enzyme may be used for studies of candidate anti-malaria reagents.

Glutathione reductase is a ubiquitous flavoenzyme involved in the protection from cell stress.

Glutathione reductase is a ubiquitous flavoenzyme involved in the protection from cell stress. Glutathione reductase catalyzes the reduction of oxidized glutathione (GSSG) to glutathione (GSH). It is essential for the glutathione redox cycle that maintains adequate levels of reduced cellular GSH, which serves as an antioxidant reacting with free radicals and organic peroxides. Glutathione is also an electron donor for glutathione peroxidases and a substrate for glutathione S-transferases contributing to the detoxification and elimination of toxic electrophilic metabolites and xenobiotics.

Solution containing 25 mM Tris-HCl, pH 7.4, 1 mM EDTA, and 50% (v/v) glycerol.

1 unit will reduce 1.0 μmole of DTNB to TNB per minute at 25 °C at pH 7.5.

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