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 |
Enzyme Information
| 1.8.5.7 |
Glutathionyl-hydroquinone reductase.
based on mapping to UniProt Q8KN33
Glutathione + 2-(glutathione-S-yl)-hydroquinone = glutathione disulfide + hydroquinone.
-!- This type of enzymes, which are found in bacteria, halobacteria, fungi, and plants, catalyze the glutathione-dependent reduction of glutathionyl-hydroquinones. -!- The enzyme from the bacterium Sphingobium chlorophenolicum can act on halogenated substrates such as 2,6-dichloro-3-(glutathione-S-yl)- hydroquinone and 2,3,5-trichloro-6-(glutathione-S-yl)-hydroquinone. -!- Substrates for these enzymes are often formed spontaneously by interaction of benzoquinones with glutathione.
|
UniProtKB Entries (1)
| Q8KN33 |
PCPF_SPHCR
Sphingobium chlorophenolicum
Glutathionyl-hydroquinone reductase PcpF
|
PDB Structure
| PDB | 4FQU |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural understanding of the glutathione-dependent reduction mechanism of glutathionyl-hydroquinone reductases.
J.Biol.Chem.
|
