Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase

Canales, José; Fernández, Ascensión; Rodrigues, Joaquim Rui; Ferreira, Rui; Ribeiro, João Meireles; Cabezas, Alicia; Costas, María Jesús; Cameselle, José Carlos

http://hdl.handle.net/10400.8/3028

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Authors

Canales, José

Fernández, Ascensión

Rodrigues, Joaquim Rui

Ferreira, Rui

Ribeiro, João Meireles

Cabezas, Alicia

Costas, María Jesús

Cameselle, José Carlos

Abstract(s)

Cyclic ADP-ribose (cADPR) metabolism in mammals is catalyzed by NAD glycohydrolases (NADases) that, besides forming ADP-ribose, form and hydrolyze the N(1)-glycosidic linkage of cADPR. Thus far, no cADPR phosphohydrolase was known. We tested rat ADP-ribose/CDP-alcohol pyrophosphatase (ADPRibase-Mn) and found that cADPR is an ADPRibase-Mn ligand and substrate. ADPRibase-Mn activity on cADPR was 65-fold less efficient than on ADP-ribose, the best substrate. This is similar to the ADP-ribose/cADPR formation ratio by NADases. The product of cADPR phosphohydrolysis by ADPRibase-Mn was N(1)-(5-phosphoribosyl)-AMP, suggesting a novel route for cADPR turnover.