CATH Classification

Domain Context

CATH Clusters

Superfamily Glutaredoxin
Functional Family Glutathione S-transferase omega-1

Enzyme Information

2.5.1.18
Glutathione transferase.
based on mapping to UniProt P78417
RX + glutathione = HX + R-S-glutathione.
-!- A group of enzymes of broad specificity. -!- R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. -!- Also catalyzes the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange. -!- Formerly EC 1.8.6.1, EC 2.5.1.12, EC 2.5.1.13, EC 2.5.1.14 and EC 4.4.1.7.
1.20.4.2
Methylarsonate reductase.
based on mapping to UniProt P78417
Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H(2)O.
-!- The product, methylarsonite, is biologically methylated by EC 2.1.1.137 to form cacodylic acid. -!- Formerly EC 1.97.1.7.
1.8.5.1
Glutathione dehydrogenase (ascorbate).
based on mapping to UniProt P78417
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.

UniProtKB Entries (1)

P78417
GSTO1_HUMAN
Homo sapiens
Glutathione S-transferase omega-1

PDB Structure

PDB 5V3Q
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
GSTO1-1 plays a pro-inflammatory role in models of inflammation, colitis and obesity.
Menon, D., Innes, A., Oakley, A.J., Dahlstrom, J.E., Jensen, L.M., Brustle, A., Tummala, P., Rooke, M., Casarotto, M.G., Baell, J.B., Nguyen, N., Xie, Y., Cuellar, M., Strasser, J., Dahlin, J.L., Walters, M.A., Burgio, G., O'Neill, L.A.J., Board, P.G.
Sci Rep