Any feedback?
Literature summary 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)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.3.1.1 | expression of the N-terminally His6-tagged enzyme in Escherichia coli strain M15 | Pyrococcus furiosus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.3.1.1 | 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
| EC Number | General Stability | Organism |
|---|---|---|
| 5.3.1.1 | destabilization of TIM by SDS at pH 3.0 | Pyrococcus furiosus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.1 | D-Glyceraldehyde 3-phosphate | Pyrococcus furiosus | - |
Glycerone phosphate | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.1.1 | Pyrococcus furiosus | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.1 | D-Glyceraldehyde 3-phosphate | - |
Pyrococcus furiosus | Glycerone phosphate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.3.1.1 | TIM | - |
Pyrococcus furiosus |
| 5.3.1.1 | Triosephosphate isomerase | - |
Pyrococcus furiosus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.1 | additional information | - |
Thermal melting of PfuTIM in buffers of different pH, overview | Pyrococcus furiosus |
| 5.3.1.1 | 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
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.1 | 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 |
| 5.3.1.1 | 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 |
| 5.3.1.1 | 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
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 5.3.1.1 | Pyrococcus furiosus | recombinant His6-tagged enzyme | - |
6.9 |
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
