Literature summary 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.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.1.1.1	-	Scaptodrosophila lebanonensis

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.1.1.1	pyrazole	competitive	Scaptodrosophila lebanonensis

Natural Substrates/ Products (Substrates)

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.1.1.1	Scaptodrosophila lebanonensis	-	-	-

Reaction

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

Substrates and Products (Substrate)

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

Cofactor

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

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Release 2023.1 (January 2023)