Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.8/3028
Título: Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase
Autor: Canales, José
Fernández, Ascensión
Rodrigues, Joaquim Rui
Ferreira, Rui
Ribeiro, João Meireles
Cabezas, Alicia
Costas, María Jesús
Cameselle, José Carlos
Palavras-chave: Adenosine Diphosphate Ribose
Animals
Cyclic ADP-Ribose
Hydrolysis
Manganese
Models, Molecular
Pyrophosphatases
Rats
Substrate Specificity
Data: 2009
Resumo: 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.
Peer review: yes
URI: http://hdl.handle.net/10400.8/3028
DOI: 10.1016/j.febslet.2009.04.023
Aparece nas colecções:Artigos em revistas internacionais

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