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 (Baker's Yeast (S. cerevisiae))
Source
Baker's yeast (S. cerevisiae)
Form
ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4, pH 7.0, containing 0.1 mM dithiothreitol
Enzyme Commission Number
EC 1.6.4.2
Activity
100-300 units/mg protein (biuret)
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.
Warnings
Purified by affinity chromatography
Function
NADP binding; flavin adenine dinucleotide binding; glutathione-disulfide reductase activity
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
Download Datasheet