Canales, JoséFernández, AscensiónRodrigues, Joaquim RuiFerreira, RuiRibeiro, João MeirelesCabezas, AliciaCostas, María JesúsCameselle, José Carlos2018-02-122018-02-122009http://hdl.handle.net/10400.8/3028Cyclic 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.engAdenosine Diphosphate RiboseAnimalsCyclic ADP-RiboseHydrolysisManganeseModels, MolecularPyrophosphatasesRatsSubstrate Specificityjournal article10.1016/j.febslet.2009.04.023