| Literature DB >> 19379742 |
José Canales1, Ascensión Fernández, Joaquim Rui Rodrigues, Rui Ferreira, João Meireles Ribeiro, Alicia Cabezas, María Jesús Costas, José Carlos Cameselle.
Abstract
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.Entities:
Mesh:
Substances:
Year: 2009 PMID: 19379742 DOI: 10.1016/j.febslet.2009.04.023
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124