Literature summary for 1.1.1.1 extracted from

Koumanov, A.; Benach, J.; Atrian, S.; Gonzalez-Duarte, R.; Karshikoff, A.; Ladenstein, R.
The catalytic mechanism of Drosophila alcohol dehydrogenase: evidence for a proton relay modulated by the coupled ionization of the active site lysine/tyrosine pair and a NAD+ ribose OH switch (2003), Proteins, 51, 289-298.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	detailed kinetics, computational analysis of the reaction mechanism	Scaptodrosophila lebanonensis

Organism

Organism	UniProt	Comment	Textmining
Scaptodrosophila lebanonensis	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
a primary alcohol + NAD+ = an aldehyde + NADH + H+	catalytic mechanism involves a proton relay modulated by the coupled ionization of the active site Lys155/Tyr151 pair, and a NAD+ ribose 2'-OH switch, other active site residues are Ser138 and Trp144, ionization properties, substrate binding, overview	Scaptodrosophila lebanonensis	a

Synonyms

Synonyms	Comment	Organism
DADH	-	Scaptodrosophila lebanonensis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
additional information	-	pH dependence of the reaction mechanism and enzyme-substrate interaction, overview	Scaptodrosophila lebanonensis

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Scaptodrosophila lebanonensis

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Release 2023.1 (January 2023)