Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Isobutyramide | competitive to N,N-dimethyl-4-nitrosoaniline | Amycolatopsis methanolica | |
trifluoroethanol | nonreactive substrate analogue, competitive to ethanol | Amycolatopsis methanolica |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Amycolatopsis methanolica | P80175 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ethanol + N,N-dimethyl-4-nitrosoaniline | - |
Amycolatopsis methanolica | acetaldehyde + 4-(hydroxylamino)-N,N-dimethylaniline | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | The NADH absorbance spectrum of nicotinoprotein alcohol dehydrogenase has a maximum at 326 nm. Reduced enzyme-bound pyridine dinucleotide can be reversibly oxidized by acetaldehyde. The fluorescence excitation spectrum for NADH bound to the enzyme has a maximum at 325 nm. Upon excitation at 290 nm, energy transfer from tryptophan to enzyme-bound NADH is negligible. The fluorescence emission spectrum upon excitation at 325 nm for NADH bound to the enzyme has a maximum at 422 nm. The fluorescence lifetime of NADH bound to the nicotinoprotein is very short compared to enzyme-bound NADH complexes, also compared to NADH bound to horse liver alcohol dehydrogenase. The cofactor-protein interaction in the nicotinoprotein alcohol dehydrogenase active site is more rigid and apolar than that in horse liver alcohol dehydrogenase | Amycolatopsis methanolica |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0016 | - |
trifluoroethanol | pH 7.0, 20°C | Amycolatopsis methanolica | |
0.046 | - |
Isobutyramide | pH 7.0, 20°C | Amycolatopsis methanolica |