GSR Human

Glutathione reductase (GR), also known as glutathione-disulfide reductase (GSR), is a crucial enzyme in cellular defense against oxidative stress. It catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH), which is essential for maintaining the reducing environment of the cell .

Glutathione reductase is a homodimeric flavoprotein disulfide oxidoreductase. Each monomer contains a flavin adenine dinucleotide (FAD) prosthetic group and utilizes NADPH as a reducing agent to convert GSSG into two molecules of GSH . This reaction is vital for the detoxification of reactive oxygen species (ROS) and maintaining cellular redox homeostasis .

The enzyme plays a critical role in the prevention of oxidative damage within the cell. By maintaining high levels of reduced glutathione, GR helps protect cellular components from oxidative stress, which can lead to cell damage and death . This function is particularly important in tissues with high oxidative metabolism, such as the liver and red blood cells .

Recombinant human glutathione reductase is produced using various expression systems, including bacterial, yeast, and mammalian cells. The recombinant form is often used in research and therapeutic applications due to its high purity and activity . The production process involves cloning the human GSR gene into an expression vector, transforming the host cells, and purifying the expressed protein .

Deficiency in glutathione reductase can lead to various health issues, including increased susceptibility to oxidative stress and hemolytic anemia . Monitoring GR activity is crucial in diagnosing and managing conditions related to oxidative stress .