Gluten enteropathy

Glutathione-disulfide reductase (GSR) is an enzyme that plays a crucial role in maintaining the antioxidant system of the body. It is primarily responsible for the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell.

Function

Glutathione-disulfide reductase catalyzes the reduction of glutathione disulfide to glutathione, a process that involves the oxidation of NADPH to NADP+. This reaction is essential for protecting the cell from reactive oxygen species such as free radicals and peroxides.

Structure

The GSR enzyme is a flavoprotein that contains a FAD molecule in its active site. The enzyme is a homodimer, with each monomer composed of a FAD-binding domain and a NADPH-binding domain.

Clinical significance

Deficiency in GSR can lead to hemolytic anemia, due to the buildup of oxidative stress in red blood cells. This condition is rare and is usually inherited in an autosomal recessive manner.

See also

• Glutathione
• Glutathione disulfide
• Oxidative stress
• Hemolytic anemia