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Hydrolysis of the phosphoanhydride linkage of cyclic ADP‐ribose by the Mn 2+ ‐dependent ADP‐ribose/CDP‐alcohol pyrophosphatase
Author(s) -
Canales José,
Fernández Ascensión,
Rodrigues Joaquim Rui,
Ferreira Rui,
Ribeiro João Meireles,
Cabezas Alicia,
Costas María Jesús,
Cameselle José Carlos
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.04.023
Subject(s) - cyclic adp ribose , pyrophosphatase , nad+ kinase , chemistry , ribose , inorganic pyrophosphatase , hydrolysis , biochemistry , substrate (aquarium) , alcohol , stereochemistry , enzyme , pyrophosphate , biology , cd38 , stem cell , cd34 , ecology , genetics
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.