Any feedback?
Literature summary extracted from
- Inhibition of the catalytic activity of alcohol dehydrogenase by nitric oxide is associated with S nitrosylation and the release of zinc (1996), Biochemistry, 35, 16186-16194.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.1 | NO | Cys residues contained within the zinc/thiolate active center may be primary sites of NO interaction | Equus caballus |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.1 | ethanol + NAD+ | Equus caballus | plays an important role in the metabolism of ethanol | acetaldehyde + NADH | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.1 | Equus caballus | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.1 | ethanol + NAD+ | - |
Equus caballus | acetaldehyde + NADH | - |
? | |
| 1.1.1.1 | ethanol + NAD+ | plays an important role in the metabolism of ethanol | Equus caballus | acetaldehyde + NADH | - |
? | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.1 | NAD+ | - |
Equus caballus | |
| 1.1.1.1 | NADH | - |
Equus caballus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
