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Literature summary for 1.1.1.85 extracted from
- Increased thermal stability against irreversible inactivation of 3-isopropylmalate dehydrogenase induced by decreased van der Waals volume at the subunit interface (2003), Protein Eng., 16, 615-621.
Protein Variants
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
Subunits
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| 3-isopropylmalate dehydrogenase | - |
Bacillus subtilis |
Temperature Stability [°C]
| 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 |
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