Binding of NADH to horse liver alcohol dehydrogenase: dependence on concentration of benzaldehyde and benzyl alcohol.
Equilibrium titration measurements of NAD+ and NADH in the presence of stoichiometric amounts of liver alcohol dehydrogenase (10(-6)N less than enzyme = coenzyme less than 10(-4)N) have been carried out by using the couple of substrates benzyl alcohol-benzaldehyde, at pH 7.0 and 8.75, in the absence and in the presence of isobutyramide. The results obtained have been unsuccessfully analyzed on the basis of the widely accepted compulsory order model which assumes functional equivalence and independence of the enzyme sites.
D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000577:Amides / Q000378:metabolism; D000818:Animals; D001547:Benzaldehydes / Q000378:metabolism*; D019905:Benzyl Alcohol; D001592:Benzyl Alcohols / Q000378:metabolism*; D001593:Benzyl Compounds / Q000378:metabolism*; D006736:Horses; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008954:Models, Biological; D009243:NAD / Q000378:metabolism*; D010084:Oxidation-Reduction
D000577:Amides; D001547:Benzaldehydes; D001592:Benzyl Alcohols; D001593:Benzyl Compounds; D009243:NAD; C030197:isobutyramide; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; D019905:Benzyl Alcohol; C032175:benzaldehyde