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Literature summary for 1.1.1.337 extracted from
- An irreversible and kinetically controlled process: thermal induced denaturation of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus (2007), Protein J., 26, 143-151.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Weissella confusa | P14295 | i.e. Lactobacillus confusus | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| L-2-hydroxyisocaproate dehydrogenase | - |
Weissella confusa |
| L-HicDH | - |
Weissella confusa |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the thermal denaturation of the enzyme is studied by Differential Scanning Calorimetry and Circular Dichroism spectroscopy. The thermal denaturation is pH dependent. The thermal denaturation is irreversible and the T(m) is dependent on the scan-rate. Stabilizing effect of NADH binding. The denaturation process of L-HicDH is kinetically determined | Weissella confusa |
| 52 | - |
heat capacity function of the enzyme shows a single peak with the T(m) values between 52.14° C and 55.89°C at pH 7.0 at different scan rates | Weissella confusa |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Weissella confusa | calculated from sequence | - |
5.06 |
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