Protein Variants | Comment | Organism |
---|---|---|
M256A | mutation increases thermostability by 6°C in comparison to wild-type | Bacillus subtilis |
M256F | mutation decreases thermostability by 4°C in comparison to wild-type | Bacillus subtilis |
M256I | no effect | Bacillus subtilis |
M256L | no effect | Bacillus subtilis |
M256V | mutation increases thermostability by 2°C in comparison to wild-type | Bacillus subtilis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | the van der Waals volume of an amino acid residue at the hydrophobic subunit interface is an important factor for the stability of the subunit-subunit interface | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
3-isopropylmalate dehydrogenase | - |
Bacillus subtilis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
The thermal denaturation processes of wild-type and mutant enzymes are irreversible under the conditions used. Mutant M256F shows two-phase denaturation curve. The hydrophobic interactions at the subunit interface are critically important for the thermostability of dimeric enzyme. | Bacillus subtilis |