CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.30 | Glutaredoxin |
|
3.40.30.10 | Glutaredoxin |
Domain Context
CATH Clusters
| Superfamily | Glutaredoxin |
| Functional Family | Glutathione S-transferase P |
Enzyme Information
| 2.5.1.18 |
Glutathione transferase.
based on mapping to UniProt P19157
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.
|
UniProtKB Entries (1)
| P19157 |
GSTP1_MOUSE
Mus musculus
Glutathione S-transferase P 1
|
PDB Structure
| PDB | 3O76 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Site-directed mutagenesis of mouse glutathione transferase P1-1 unlocks masked cooperativity, introduces a novel mechanism for 'ping pong' kinetic behaviour, and provides further structural evidence for participation of a water molecule in proton abstraction from glutathione.
Febs J.
|
