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Literature summary extracted from
- Multifunctionality of liver alcohol dehydrogenase: kinetic and mechanistic studies of esterase reaction (1982), Arch. Biochem. Biophys., 213, 635-642.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.1 | octanoic acid | competitive inhibition of the hydrolysis of p-nitrophenyl octanoate | Equus caballus |  |
| 1.1.1.1 | p-nitrophenol | noncompetitive inhibition of the hydrolysis of p-nitrophenyl octanoate | Equus caballus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.1 | Equus caballus | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.1.1.1 | liver | - |
Equus caballus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.1 | 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]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.1 | 0.24 | - |
p-nitrophenyl octanoate | - |
Equus caballus | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.1 | NAD+ | - |
Equus caballus | |
| 1.1.1.1 | NADH | - |
Equus caballus | |
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Release 2023.1 (January 2023)
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