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http://hdl.handle.net/10174/5804
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| Title: | Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase |
| Authors: | Canales, J
Fernández, A
Rodrigues, JR
Ferreira, R
Meireles Ribeiro, J
Cabezas, A
Costas, MJ
Cameselle, JC |
| Keywords: | Cyclic ADP-ribose
ADP-ribose
Pyrophosphatase
Phosphoribosyl-AMP
Histidine biosynthesis
Immune signaling |
| Issue Date: | May-2009 |
| Citation: | Canales J, Fernández A, Rodrigues JR, Ferreira R, Meireles Ribeiro J, Cabezas A, Costas MJ, Cameselle JC (2009) - Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase, FEBS Letters 583, 1593–1598 (doi:10.1016/j.febslet.2009.04.023) |
| 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. |
| URI: | http://www.febsletters.org/article/S0014-5793(09)00297-X/abstract
http://hdl.handle.net/10174/5804 |
| Type: | article |
| Appears in Collections: | QUI - Publicações - Artigos em Revistas Internacionais Com Arbitragem Científica
MED - Publicações - Artigos em Revistas Internacionais Com Arbitragem Científica
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