CATH Classification

Domain Context

CATH Clusters

Superfamily 1.20.1050.10
Functional Family Glutathione S-transferase A1

Enzyme Information

2.5.1.18
Glutathione transferase.
based on mapping to UniProt P04903
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.
2.5.1.18
Glutathione transferase.
based on mapping to UniProt P08263
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.
1.11.1.-
Peroxidases.
based on mapping to UniProt P08263
5.3.3.-
Transposing C=C bonds.
based on mapping to UniProt P08263

UniProtKB Entries (2)

P04903
GSTA2_RAT
Rattus norvegicus
Glutathione S-transferase alpha-2
P08263
GSTA1_HUMAN
Homo sapiens
Glutathione S-transferase A1

PDB Structure

PDB 5LD0
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Directed evolution of glutathione transferases towards a selective glutathione-binding site and improved oxidative stability.
Axarli, I., Muleta, A.W., Chronopoulou, E.G., Papageorgiou, A.C., Labrou, N.E.
Biochim. Biophys. Acta