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Literature summary for 1.1.99.36 extracted from

  • Piersma, S.R.; Visser, A.J.; de Vries, S.; Duine, J.A.
    Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase (1998), Biochemistry, 37, 3068-3077.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Isobutyramide competitive to N,N-dimethyl-4-nitrosoaniline Amycolatopsis methanolica
trifluoroethanol nonreactive substrate analogue, competitive to ethanol Amycolatopsis methanolica

Organism

Organism UniProt Comment Textmining
Amycolatopsis methanolica P80175
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ethanol + N,N-dimethyl-4-nitrosoaniline
-
Amycolatopsis methanolica acetaldehyde + 4-(hydroxylamino)-N,N-dimethylaniline
-
?

Cofactor

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 [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