CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.20 | Up-down Bundle | |
1.20.1050 | Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 | |
1.20.1050.10 |
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 | 5LCZ |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Directed evolution of glutathione transferases towards a selective glutathione-binding site and improved oxidative stability.
Biochim. Biophys. Acta
|