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Literature summary for 5.3.1.1 extracted from
- Attenuation of ionic interactions profoundly lowers the kinetic thermal stability of Pyrococcus furiosus triosephosphate isomerase (2009), Biochim. Biophys. Acta, 1794, 905-912.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of the N-terminally His6-tagged enzyme in Escherichia coli strain M15 | Pyrococcus furiosus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R111T/R112A/E114K/E115G | site-directed mutagenesis, destroying of four ion pair interactions by replacing four of the charged residues in helix 4 with structurally analogous residues from the psychrophile Methanococcoides burtonii TIM to create a mutant, mPfuTIM, that is less kinetically stable than wild-type PfuTIM | Pyrococcus furiosus |
General Stability
| General Stability | Organism |
|---|---|
| destabilization of TIM by SDS at pH 3.0 | Pyrococcus furiosus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-Glyceraldehyde 3-phosphate | Pyrococcus furiosus | - |
Glycerone phosphate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-Glyceraldehyde 3-phosphate | - |
Pyrococcus furiosus | Glycerone phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| TIM | - |
Pyrococcus furiosus |
| Triosephosphate isomerase | - |
Pyrococcus furiosus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
Thermal melting of PfuTIM in buffers of different pH, overview | Pyrococcus furiosus |
| 25 | 95 | no or limited loss of activity at pH 7.0 and pH 10.0, respectively, 50% loss of activity at pH 3.0. Cooling from 95°C induces cold denaturation in partially denatured TIM | Pyrococcus furiosus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3 | - |
from 25 to 95°C, profound unfolding and loss of 50% activity occurs at pH 3.0, also when the enzyme is directly placed at 95°C during 150 s. TIM has similar secondary structure but different surface features at pH 3.0, and shows increased susceptibility to thermal unfolding at pH 3.0 | Pyrococcus furiosus |
| 7 | - |
25-95°C with slow elevation of temperature, no loss of activity, also no loss when the enzyme is directly placed at 95°C during 150 s | Pyrococcus furiosus |
| 10 | - |
25-95°C with slow elevation of temperature, limited loss of activity, also no loss when the enzyme is directly placed at 95°C during 150 s | Pyrococcus furiosus |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Pyrococcus furiosus | recombinant His6-tagged enzyme | - |
6.9 |
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