Glutathione S Transferase Omega 1 (GSTo1)

Glutathione S-transferase omega-1 is an enzyme that  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.This protein has dehydroascorbate reductase activity and may function in the glutathione-ascorbate cycle as part of antioxidant metabolism.

GSTO1 has an N-terminal thioredoxin-like domain consisting of a central 4-stranded beta sheet flanked on one side by 2 alpha helices and on the other by a 3-10 helix. The C terminus is composed of 7 alpha helices and makes several H bonds with the N-terminal domain. GSTO1 forms a dimer and adopts the typical GST tertiary structure.