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  • Title: Involvement of bovine spleen NAD+ glycohydrolase in the metabolism of cyclic ADP-ribose-mechanism of the cyclization reaction.
    Author: Muller-Steffner H, Augustin A, Schuber F.
    Journal: Adv Exp Med Biol; 1997; 419():399-409. PubMed ID: 9193682.
    Abstract:
    We have shown that highly purified bovine spleen NAD+ glycohydrolase (NADase), known so far to catalyze the hydrolysis of the nicotinamide-ribose bond of NAD(P)+, was also able to convert NAD+ into cyclic ADP-ribose (cADPR) and to hydrolyze cADPR into ADP-ribose. The kinetic parameters measured for the cyclic ADP-ribose hydrolase activity seem to exclude that cADPR is a kinetically competent reaction intermediate in the NADase catalyzed conversion of NAD+ into ADP-ribose. The cyclase activity of bovine NADase was best evidenced by the transformation of NGD+ into cyclic GDP-ribose which was the major reaction product whereas, in contrast, cADPR accounted for less than 2% of the products formed. For the formation of cADPR we propose a reaction mechanism that is based on the partitioning of an oxocarbenium reaction intermediate between an intramolecular attack by the N1-position of adenine and an intramolecular reaction by a water molecule. Accordingly, the difference in cyclization between NAD+ and NGD+ is accounted for by the difference in reactivity of the N1 and N7 positions of the purine ring in these dinucleotides.
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