Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase
Autor(a) principal: | |
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Data de Publicação: | 2009 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10174/5804 |
Resumo: | 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. |
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Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphataseCyclic ADP-riboseADP-ribosePyrophosphatasePhosphoribosyl-AMPHistidine biosynthesisImmune signalingCyclic 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.2012-11-20T15:22:00Z2012-11-202009-05-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10174/5804http://hdl.handle.net/10174/5804porCanales 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)http://www.febsletters.org/article/S0014-5793(09)00297-X/abstractICAAMndndndraf@uevora.ptndndndnd365Canales, JFernández, ARodrigues, JRFerreira, RMeireles Ribeiro, JCabezas, ACostas, MJCameselle, JCinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-01-03T18:44:37Zoai:dspace.uevora.pt:10174/5804Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T01:00:39.546381Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase |
title |
Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase |
spellingShingle |
Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase Canales, J Cyclic ADP-ribose ADP-ribose Pyrophosphatase Phosphoribosyl-AMP Histidine biosynthesis Immune signaling |
title_short |
Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase |
title_full |
Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase |
title_fullStr |
Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase |
title_full_unstemmed |
Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase |
title_sort |
Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase |
author |
Canales, J |
author_facet |
Canales, J Fernández, A Rodrigues, JR Ferreira, R Meireles Ribeiro, J Cabezas, A Costas, MJ Cameselle, JC |
author_role |
author |
author2 |
Fernández, A Rodrigues, JR Ferreira, R Meireles Ribeiro, J Cabezas, A Costas, MJ Cameselle, JC |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Canales, J Fernández, A Rodrigues, JR Ferreira, R Meireles Ribeiro, J Cabezas, A Costas, MJ Cameselle, JC |
dc.subject.por.fl_str_mv |
Cyclic ADP-ribose ADP-ribose Pyrophosphatase Phosphoribosyl-AMP Histidine biosynthesis Immune signaling |
topic |
Cyclic ADP-ribose ADP-ribose Pyrophosphatase Phosphoribosyl-AMP Histidine biosynthesis Immune signaling |
description |
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. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-05-01T00:00:00Z 2012-11-20T15:22:00Z 2012-11-20 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10174/5804 http://hdl.handle.net/10174/5804 |
url |
http://hdl.handle.net/10174/5804 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
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) http://www.febsletters.org/article/S0014-5793(09)00297-X/abstract ICAAM nd nd nd raf@uevora.pt nd nd nd nd 365 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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