Abstract
Abstract The substrate specificity of bull semen NAD nucleosidase for various NAD analogs was studied. It was found that NAD, NADP, and nicotinamide hypoxanthine dinucleotide served well as substrates for the enzyme. The enzyme also catalyzed the hydrolysis of nicotinamide mononucleotide, 3-acetylpyridine adenine dinucleotide, 3-acetylpyridine hypoxanthine dinucleotide, 3-pyridinealdehyde adenine dinucleotide, thionicotinamide adenine dinucleotide, and 3-pyridinealdehyde hypoxanthine dinucleotide but at much slower rates. The hydrolysis of NADH, NADPH, and α-NAD was found not to be catalyzed by the enzyme. The enzyme was observed to be inhibited noncompetitively in the presence of nicotinamide; however, it was observed not to catalyze a pyridine base exchange reaction. Product inhibition patterns with nicotinamide and adenosine diphosphoribose were consistent with an Ordered Uni Bi reaction in which nicotinamide is the first product released by the enzyme.
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