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Glutathione S-transferase A3 is an enzyme that in humans is encoded by the GSTA3 gene. [5] [6] [7] Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds.
Glutathione synthetase deficiency has an autosomal recessive pattern of inheritance. Mutations in the GSS gene cause glutathione synthetase deficiency. This gene provides instructions for making the enzyme glutathione synthetase. This enzyme is involved in a process called the gamma-glutamyl cycle, which takes place in most of the body's cells ...
[12] [13] Therefore, if a human glutathione S-transferase is a homodimer in the pi-class subfamily 1, its name will be written as "hGSTP1-1." The early nomenclature for GSTs referred to them as “Y” proteins, referring to their separation in the “Y” fraction (as opposed to the “X and Z” fractions) using Sephadex G75 chromatography. [14]
Glutathione S-transferase omega-1 is an enzyme that in humans is encoded by the GSTO1 gene. [5] [6] [7] This gene encodes a member of the theta class glutathione S-transferase-like (GSTTL) protein family. In mouse, the encoded protein acts as a small stress response protein, likely involved in cellular redox homeostasis. [7]
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After the final GSH product is made, it can be used by glutathione peroxidase to neutralize reactive oxygen species (ROS) such as H 2 O 2 or Glutathione S-transferases in the detoxification of xenobiotics. [7] Reaction mechanism for GSH biosynthesis. [14] Glutamate and cysteine side chains are shown in red and green, respectively.