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Literature summary for 2.7.2.3 extracted from
- Stability domains, substrate-induced conformational changes and hinge-bending motions in a psychrophilic phosphoglycerate kinase: A microcalorimetric study (2005), J. Biol. Chem., 280, 41307-41314.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas sp. | - |
TACII18 | - |
| Pseudomonas sp. TACII18 | - |
TACII18 | - |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the psychrophilic enzyme enzyme exhibits two distinct stability domains in the free, open conformation. These stability domains do not match the structural N- and C-domains as the heat-stable domain corresponds to about 80 residues of the C-domain, including the nucleotide binding site, whereas the remaining of the protein contributes to the main heat-labile domain | Pseudomonas sp. |
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