ENZYME entry: EC 1.1.99.36
| Accepted Name |
|---|
| Alcohol dehydrogenase (nicotinoprotein).
|
| Alternative Name(s) |
|---|
| NDMA-dependent alcohol dehydrogenase. |
| Nicotinoprotein alcohol dehydrogenase. |
| Reaction catalysed |
|---|
| Ethanol + acceptor <=> acetaldehyde + reduced acceptor |
| Cofactor(s) |
|---|
| Zn(2+).
|
| Comment(s) |
|---|
- Nicotinoprotein alcohol dehydrogenases are unique medium-chain
dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a
tightly bound NAD(+)/NADH cofactor that does not dissociate during
the catalytic process.
- Instead, the cofactor is regenerated by a second substrate or
electron carrier.
- While the in vivo electron acceptor is not known, N,N-dimethyl-4-
nitrosoaniline (NDMA) can serve this function in vitro.
- The enzyme from the Gram-positive bacterium Amycolatopsis methanolica
can accept many primary alcohols as substrates, including
benzylalcohol.
|
| Cross-references |
|---|
| BRENDA | 1.1.99.36 |
| EC2PDB | 1.1.99.36 |
| ExplorEnz | 1.1.99.36 |
| PRIAM enzyme-specific profiles | 1.1.99.36 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.1.99.36 |
| IUBMB Enzyme Nomenclature | 1.1.99.36 |
| IntEnz | 1.1.99.36 |
| MEDLINE | Find literature relating to 1.1.99.36 |
| MetaCyc | 1.1.99.36 |
| UniProtKB/Swiss-Prot |
|
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