Glutathione S-transferase A1
Domain
The C-terminal domain may form a component of the hydrophobic substrate-binding site, but in contrast appears not to be directly involved in GSH binding and is not absolutely essential for catalytic activity.
Function
Glutathione S-transferase that catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of exogenous and endogenous compounds (Probable). Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2) (PubMed:9084911). It also catalyzes the isomerization of D5-androstene-3,17-dione (AD) into D4-androstene-3,17-dione and may therefore play an important role in hormone biosynthesis (PubMed:11152686). Through its glutathione-dependent peroxidase activity toward the fatty acid hydroperoxide (13S)-hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE it is also involved in the metabolism of oxidized linoleic acid (PubMed:16624487).
Sequence Similarities
Belongs to the GST superfamily. Alpha family.
Tissue Specificity
Liver.
Cellular localization
- Cytoplasm
Alternative names
Glutathione S-transferase A1, 13-hydroperoxyoctadecadienoate peroxidase, GST HA subunit 1, GST class-alpha member 1, GST-epsilon, GSTA1-1, GTH1, GSTA1