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Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-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

Date: 2009

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

Origin: IC-online

Subject(s): Adenosine Diphosphate Ribose; Animals; Cyclic ADP-Ribose; Hydrolysis; Manganese; Models, Molecular; Pyrophosphatases; Rats; Substrate Specificity; Adenosine Diphosphate Ribose; Adenosine Diphosphate Ribose; Animals; Animals; Cyclic ADP-Ribose; Cyclic ADP-Ribose; Hydrolysis; Hydrolysis; Manganese; Manganese; Models, Molecular; Models, Molecular; Pyrophosphatases; Pyrophosphatases; Rats; Rats; Substrate Specificity; Substrate Specificity

Description

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.

Document Type Journal article
Language English
Contributor(s) Repositório IC-Online

Document details

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

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