Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase

Detalhes bibliográficos
Autor(a) principal: Canales, J
Data de Publicação: 2009
Outros Autores: Fernández, A, Rodrigues, JR, Ferreira, R, Meireles Ribeiro, J, Cabezas, A, Costas, MJ, Cameselle, JC
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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spelling 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
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution 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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