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Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn-dependent ADP-ribose/CDP-alcohol pyrophosphatase |
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| Authors: | José Canales Joaquim Rui Rodrigues João Meireles Ribeiro María Jesús Costas |
| Institution: | a Grupo de Enzimología, Departamento de Bioquímica y Biología Molecular y Genética, Facultad de Medicina, Universidad de Extremadura, Apartado 108, E-06080 Badajoz, Spain b Escola Superior de Tecnologia e Gestão, Instituto Politécnico de Leiria, Leiria, Portugal c Departamento de Química, Universidade de Évora, Évora, Portugal |
| Abstract: | Cyclic ADP-ribose (cADPR) metabolism in mammals is catalyzed by NAD glycohydrolases (NADases) that, besides forming ADP-ribose, form and hydrolyze the N1-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 N1-(5-phosphoribosyl)-AMP, suggesting a novel route for cADPR turnover. |
| Keywords: | ADPRibase-Mn Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase cADPR cyclic ADP-ribose DMSO dimethylsulfoxide NADase NAD glycohydrolase pRib-Ado N1-(5-phosphoribosyl)-adenosine pRib-AMP N1-(5-phosphoribosyl)-adenosine 5&prime -monophosphate pRib-ATP N1-(5-phosphoribosyl)-adenosine 5&prime -triphosphate Rib-Ado N1-(ribosyl)-adenosine Rib-AMP N1-(ribosyl)-adenosine 5&prime -monophosphate |
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