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Literature summary for 1.1.1.1 extracted from
- Thermal inactivation and conformational lock studies on horse liver alcohol dehydrogenase: structural mechanism (2013), Int. J. Biol. Macromol., 58, 66-72.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Equus caballus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Equus caballus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ethanol + NAD+ | - |
Equus caballus | acetaldehyde + NADH + H+ | - |
? |  |
Temperature Stability [°C]
| 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 |
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