Any feedback?
Literature summary for 2.4.1.1 extracted from
- Effect of proline on thermal inactivation, denaturation and aggregation of glycogen phosphorylase b from rabbit skeletal muscle (2009), Biophys. Chem., 141, 66-74.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| proline | concentrations of 0.1 M have a slight accelerating effect on thermal aggregation of glycogen phosphorylase b. The suppression aggregation at high proline concentrations is mainly due to the protective action of proline on the stage of unfolding of the molecule | Oryctolagus cuniculus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
glycogen phosphorylase b | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| skeletal muscle | - |
Oryctolagus cuniculus | - |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 48 | - |
half-life about 50 min. In presence of 1.5 M proline, half-life above 150 min. Suppression of thermal aggregation at high proline concentrations is mainly due to the protective action of proline on the stage of unfolding of the molecule | Oryctolagus cuniculus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
