Activating Compound | Comment | Organism | Structure |
---|---|---|---|
DTT | - |
Thermus thermophilus |
Cloned (Comment) | Organism |
---|---|
expressed as His-tagged and non-His-tagged fusion proteins in Escherichia coli | Thermus thermophilus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | - |
Thermus thermophilus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
73300 | - |
SDS-PAGE | Thermus thermophilus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | Q5SIY4 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-isopropylmalate + NAD+ | - |
Thermus thermophilus | 2-ketoisocaproate + NADH + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
3-isopropylmalate dehydrogenase | - |
Thermus thermophilus |
IPMDH | - |
Thermus thermophilus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
time-dependent denaturation-renaturation experiments on IPMDH are presented. Unfolding occurs in a single first-order step with half-times of 1 h. The binding of Mn*IPM (the manganese complex of 3-isopropylmalate) markedly reduces the rates of unfolding. Refolding is a two-step or multistep first-order process involving an inactive intermediate. The restoration of the native structure and reactivation take place with a half-time of a few min | Thermus thermophilus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
- |
Thermus thermophilus |