Any feedback?
Literature summary for 5.3.1.1 extracted from
- Complex kinetics and residual structure in the thermal unfolding of yeast triosephosphate isomerase (2015), BMC Biochem., 16, 20 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| thermally unfolded protein refolds faster at pH 6.7 than at pH 8.0 and TIM refolds faster from the denatured state with residual structure | Saccharomyces cerevisiae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
slow temperature-induced unfolding of yeast TIM shows three kinetic phases. A complex mechanism involving off-pathway intermediates or parallel pathways may be operating. beta-Strand-type residual structure appears below pH 8.0, and is likely to be associated with increased irreversible aggregation of the unfolded protein, which accelerates the refolding process | Saccharomyces cerevisiae |
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
