Description
Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl proteases, Citrate synthase, EF hands, hemoglobins, lipecalins, and α/β hydrolases. GR is stimulated by melatonin and is reportedly irreversibly inhibited by a number of oxygen radical generating systems.
Abbr
GR, Native (Spinach)
Form
ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4 mM, 10 mM potassium phosphate, pH 7.0
Enzyme Commission Number
EC 1.6.4.2
Activity
100-200 units/mg protein
Molecular Weight
mol wt 118 kDa
Unit Definition
One unit will reduce 1.0 μmole of oxidized glutathione per min at pH 7.6 at 25°C. (Protein determined by biuret).
Synonyms
EC 1.6.4.2; 9001-48-3; Glutathione Reductase; GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase
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