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Literature summary for 1.1.1.1 extracted from
- Multifunctionality of liver alcohol dehydrogenase: kinetic and mechanistic studies of esterase reaction (1982), Arch. Biochem. Biophys., 213, 635-642.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| octanoic acid | competitive inhibition of the hydrolysis of p-nitrophenyl octanoate | Equus caballus |  |
| p-nitrophenol | noncompetitive inhibition of the hydrolysis of p-nitrophenyl octanoate | Equus caballus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Equus caballus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Equus caballus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| p-nitrophenyl octanoate + H2O | acid-assisted nucleophilic catalysis involving the ammonium ion of Lys and the thiolate of Cys in the acyl-oxygen cleavage | Equus caballus | p-nitrophenol + octanoate | - |
? | |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.24 | - |
p-nitrophenyl octanoate | - |
Equus caballus | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Equus caballus | |
| NADH | - |
Equus caballus | |
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