1.1.1.1	a primary alcohol + NAD+ = an aldehyde + NADH + H+	active site structure	656525	
1.1.1.1	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	657317	
1.1.1.1	a primary alcohol + NAD+ = an aldehyde + NADH + H+	class IV alcohol dehydrogenase also functions as retinol dehydrogenase, reaction and kinetic mechanism: asymmetric rapid equilibrium random mechanism with 2 dead-end ternary complexes fro retinol oxidation and a rapid equilibrium ordered mechanism with one dead-end ternary complex for retinal reduction, a unique mechanistic form fro zinc-containing ADH in the medium chain dehydrogenase/reductase superfamily of enzymes	656058	
1.1.1.1	a primary alcohol + NAD+ = an aldehyde + NADH + H+	compulsory-order mechanism with the rate-limiting step being the dissociation of the product enzyme-NAD+ complex	285645	
1.1.1.1	a primary alcohol + NAD+ = an aldehyde + NADH + H+	detailed determination of the reaction and kinetic mechanisms, active site structure and determination of amino acid residues involved in catalysis, 3 isozymes	655649	
1.1.1.1	a primary alcohol + NAD+ = an aldehyde + NADH + H+	isoenzyme EE and SS: ordered bi bi mechanism	285590	
1.1.1.1	a primary alcohol + NAD+ = an aldehyde + NADH + H+	kinetic mechanism is random for ethanol oxidation and compulsory ordered for acetaldehyde reduction	285596	
1.1.1.1	a primary alcohol + NAD+ = an aldehyde + NADH + H+	mechanism is predominantly ordered with ethanol, but partially random with butanol	285646	
1.1.1.1	a primary alcohol + NAD+ = an aldehyde + NADH + H+	ordered bi bi mechanism with cofactor adding first to form a binary enzyme complex	285578	
1.1.1.1	a primary alcohol + NAD+ = an aldehyde + NADH + H+	ordered bi-bi mechanism	285586, 285598