Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase
| dc.contributor.author | Canales, J | |
| dc.contributor.author | Fernández, A | |
| dc.contributor.author | Rodrigues, JR | |
| dc.contributor.author | Ferreira, R | |
| dc.contributor.author | Meireles Ribeiro, J | |
| dc.contributor.author | Cabezas, A | |
| dc.contributor.author | Costas, MJ | |
| dc.contributor.author | Cameselle, JC | |
| dc.date.accessioned | 2012-11-20T15:22:00Z | |
| dc.date.available | 2012-11-20T15:22:00Z | |
| dc.date.issued | 2009-05 | |
| dc.description.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. | por |
| dc.identifier.authoremail | nd | |
| dc.identifier.authoremail | nd | |
| dc.identifier.authoremail | nd | |
| dc.identifier.authoremail | raf@uevora.pt | |
| dc.identifier.authoremail | nd | |
| dc.identifier.authoremail | nd | |
| dc.identifier.authoremail | nd | |
| dc.identifier.authoremail | nd | |
| dc.identifier.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) | por |
| dc.identifier.scientificarea | 365 | por |
| dc.identifier.sharewith | ICAAM | por |
| dc.identifier.uri | http://www.febsletters.org/article/S0014-5793(09)00297-X/abstract | |
| dc.identifier.uri | http://hdl.handle.net/10174/5804 | |
| dc.language.iso | por | por |
| dc.peerreviewed | yes | por |
| dc.rights | openAccess | por |
| dc.subject | Cyclic ADP-ribose | por |
| dc.subject | ADP-ribose | por |
| dc.subject | Pyrophosphatase | por |
| dc.subject | Phosphoribosyl-AMP | por |
| dc.subject | Histidine biosynthesis | por |
| dc.subject | Immune signaling | por |
| dc.title | Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase | por |
| dc.type | article | por |
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