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EC Tree
IUBMB Comments A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
The taxonomic range for the selected organisms is: Sulfolobus sp. The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
adh, alcohol dehydrogenase, aldehyde dehydrogenase, adh1b, short-chain dehydrogenase/reductase, ssadh, adh1c, yeast alcohol dehydrogenase, retinol dehydrogenase, faldh,
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alcohol dehydrogenase (NAD)
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Alcohol dehydrogenase-B2
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aldehyde reductase
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aliphatic alcohol dehydrogenase
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dehydrogenase, alcohol
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ethanol dehydrogenase
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Gastric alcohol dehydrogenase
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Glutathione-dependent formaldehyde dehydrogenase
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NAD-dependent alcohol dehydrogenase
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NAD-specific aromatic alcohol dehydrogenase
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NADH-alcohol dehydrogenase
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NADH-aldehyde dehydrogenase
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Octanol dehydrogenase
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primary alcohol dehydrogenase
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Retinol dehydrogenase
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yeast alcohol dehydrogenase
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KEGG
alpha-Linolenic acid metabolism , Biosynthesis of secondary metabolites , Chloroalkane and chloroalkene degradation , Drug metabolism - cytochrome P450 , Fatty acid degradation , Glycine, serine and threonine metabolism , Glycolysis / Gluconeogenesis , Metabolism of xenobiotics by cytochrome P450 , Microbial metabolism in diverse environments , Naphthalene degradation , Pyruvate metabolism , Retinol metabolism , Tyrosine metabolism
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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alcohol:NAD+ oxidoreductase
A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
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benzyl alcohol + NAD+
benzaldehyde + NADH + H+
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ethanol + NAD+
acetaldehyde + NADH + H+
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0.0145
benzylalcohol
in 50 mM glycine-NaOH at pH 10.0
0.0172
ethanol
in 50 mM glycine-NaOH at pH 10.0
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0.22
crude extract, at pH 10.0
2.88
after 12.9fold purification, at pH 10.0
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UniProt
brenda
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35000
4 * 35000, gel filtration
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homotetramer
4 * 35000, gel filtration
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85 - 90
half-life of 3 h at 85°C and 1 h at 90°C
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HiLoad Superdex 200 gel filtration
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expressed in Escherichia coli
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Cannio, R.; Fiorentino, G.; Carpinelli, P.; Rossi, M.; Bartolucci, S.
Cloning and overexpression in Escherichia coli of the genes encoding NAD-dependent alcohol dehydrogenase from two Sulfolobus species
J. Bacteriol.
178
301-305
1996
Saccharolobus solfataricus, Sulfolobus sp. (P50381), Sulfolobus sp., Sulfolobus sp. RC3 (P50381)
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