Organism | UniProt | Comment | Textmining |
---|---|---|---|
Equus caballus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Equus caballus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ethanol + NAD+ | - |
Equus caballus | acetaldehyde + NADH + H+ | - |
? |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
thermal denaturation starts above 45°C. The conformational lock number is 2 when calculated both experimentally and computationally. The enzyme becomes monomer at 46°C, its activity starts to decrease at this temperature. The activity decreases to only 11% of the native ADH activity with a two-phase manner at 49°C. The subunits are dissociated and several intermediates appear | Equus caballus |