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. 2021 Oct 11;97(8):423–461. doi: 10.2183/pjab.97.022

Figure 9.

Figure 9.

Important amino acids in the cADPR metabolism in CD38 (adapted from Ref. 86). CD38 catalyzes the formation of cADPR from NAD+ and hydrolysis of cADPR to ADPR.80) Lys-129 of CD38 is the cADPR binding site and ATP competes with cADPR for the binding site, resulting in the inhibition of the hydrolysis of cADPR.86) [Enzyme-cADPR*] is suggested to be an enzyme-stabilized ADP-ribosyl oxocarbonium ion intermediate. The intermediate is thought to be attacked by H2O to form ADPR. Cys-119 and Cys-201 are essential for the hydrolysis reaction.82) Glu-226 is essential for ADP-ribosyl cyclase.289)