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Literature summary for 1.11.1.9 extracted from
- New insight into the role of glutathione reductase in glutathione peroxidase-like activity determination by coupled reductase assay Molecular docking study (2021), J. Inorg. Biochem., 215, 111276 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| molecular docking study of interactions between 15 selenenylsulfide compounds that mimic glutathione peroxidase and the active site of glutathione reductase by molecular docking. The reduction of selenenylsulfide by glutathione reductase is important in GPx-like activity determination of GPx mimics | synthetic construct |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| synthetic construct | - |
- |
- |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | organoselenium compounds such as substituted salicyloyl 5-seleninic acids may act as possible GPx mimics. For active compounds to be reduced by glutathione reductase, Root Mean Square Distances representing 3 interatomic distances (Sligand-SCys-58, Sligand-NHis-467 and Seligand-NHis-467) necessary for the catalytic interaction with glutathione reductase are below 4.7A and docking scores are within 74-81 Kcal/mol | synthetic construct |
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Release 2023.1 (January 2023)
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