Interactions of 3-Aminopyridine Adenine Dinucleotide with Dehydrogenases

NAD was converted chemically to 3-aminopyridine adenine dinucleotide through the Hofmann hypobromite reaction and the resulting dinucleotide was purified by means of ion exchange chromatography. Spectrophotometric and fluorometric properties of the analog were studied. The 3-aminopyridine adenine dinucleotide was shown to be a competitive inhibitor in reactions catalyzed by seven NAD(P)-dependent enzymes. The 3-aminopyridine adenine dinucleotide was diazotized with the use of nitrous acid. The diazotized derivative was shown to be a site-specific inactivator of yeast alcohol dehydrogenase. Diazotized 3-amino-1-methylpyridinium chloride was prepared and shown to be less effective in the inactivation of this enzyme.