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Literature summary for 1.1.1.1 extracted from

  • Benach, J.; Atrian, S.; Gonzalez-Duarte, R.; Ladenstein, R.
    The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography (1999), J. Mol. Biol., 289, 335-355.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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Scaptodrosophila lebanonensis

Inhibitors

Inhibitors Comment Organism Structure
pyrazole competitive Scaptodrosophila lebanonensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Scaptodrosophila lebanonensis the enzyme oxidizes alcohols to aldehydes or ketones both for detoxification and metabolic purposes ?
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?

Organism

Organism UniProt Comment Textmining
Scaptodrosophila lebanonensis
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-
-

Reaction

Reaction Comment Organism Reaction ID
a primary alcohol + NAD+ = an aldehyde + NADH + H+ Theorell-Chance mechanism Scaptodrosophila lebanonensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme oxidizes alcohols to aldehydes or ketones both for detoxification and metabolic purposes Scaptodrosophila lebanonensis ?
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?

Cofactor

Cofactor Comment Organism Structure
additional information crystallographic study of the coenzyme binding mode Scaptodrosophila lebanonensis
NAD+
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Scaptodrosophila lebanonensis
NADH
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Scaptodrosophila lebanonensis