Activity of NMN+, nicotinamide ribose and analogs in alcohol oxidation promoted by horse-liver alcohol dehydrogenase. Improvement of this activity and structural requirements of the pyridine nucleotide part of the NAD+ coenzyme.

Kinetic constants of horse-liver alcohol-dehydrogenase-mediated oxidation of alcohol by nicotinamide mononucleotide and nicotinamide ribose were determined and the role of different adenine moieties complementing the reaction mixtures was investigated. Five nicotinamide ribose analogs were synthesized and their activities as NAD+ inhibitors and as cofactors in this dehydrogenase-mediated oxidation of alcohol were assayed. In the light of these results, structural requirements of the pyridine ribofuranosyl part of the NAD+ are discussed.