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Literature summary for 5.3.99.2 extracted from
- Effects of removing a conserved disulfide bond on the biological characteristics of rat lipocalin-type prostaglandin D synthase (2008), Biochimie, 90, 1637-1646.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C186A | no significant change in conformation. Decrease in stability and in dissociation constants for 8-anilino-1-naphthalenesulfonic acid and retinoic acid. Urea-induced unfolding at 2.875 mol/l compared with 5.75 mol/l for wild-type | Rattus norvegicus |
| C65A | no significant change in conformation. Urea-induced unfolding at 5.125 mol/l compared with 5.75 mol/l for wild-type | Rattus norvegicus |
| C89A/C186A | no significant change in conformation. Decrease in stability and in dissociation constants for 8-anilino-1-naphthalenesulfonic acid. Urea-induced unfolding at 2.625 mol/l compared with 5.75 mol/l for wild-type | Rattus norvegicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 57.4 | - |
melting temperature, mutant C89A/C186A | Rattus norvegicus |
| 59.6 | - |
melting temperature, mutant C186A | Rattus norvegicus |
| 69.3 | - |
melting temperature, wild-type | Rattus norvegicus |
| 69.4 | - |
melting temperature, mutant C65A | Rattus norvegicus |
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Release 2023.1 (January 2023)
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