Hydrolysis of the phosphoanhydride linkage of cyclic ADP‐ribose by the Mn2+‐dependent ADP‐ribose/CDP‐alcohol pyrophosphatase
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) a...
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| Published in | FEBS letters Vol. 583; no. 10; pp. 1593 - 1598 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
19.05.2009
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| Abstract | 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. |
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| AbstractList | 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. |
| Author | Cabezas, Alicia Cameselle, José Carlos Fernández, Ascensión Costas, María Jesús Ribeiro, João Meireles Canales, José Ferreira, Rui Rodrigues, Joaquim Rui |
| Author_xml | – sequence: 1 givenname: José surname: Canales fullname: Canales, José – sequence: 2 givenname: Ascensión surname: Fernández fullname: Fernández, Ascensión – sequence: 3 givenname: Joaquim Rui surname: Rodrigues fullname: Rodrigues, Joaquim Rui – sequence: 4 givenname: Rui surname: Ferreira fullname: Ferreira, Rui – sequence: 5 givenname: João Meireles surname: Ribeiro fullname: Ribeiro, João Meireles – sequence: 6 givenname: Alicia surname: Cabezas fullname: Cabezas, Alicia – sequence: 7 givenname: María Jesús surname: Costas fullname: Costas, María Jesús – sequence: 8 givenname: José Carlos surname: Cameselle fullname: Cameselle, José Carlos email: camselle@unex.es |
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| Copyright | FEBS Letters 583 (2009) 1873-3468 © 2015 Federation of European Biochemical Societies |
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| SubjectTerms | ADP-ribose ADPRibase-Mn cADPR cyclic ADP-ribose dimethylsulfoxide DMSO Histidine biosynthesis Immune signaling Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase N 1-(5-phosphoribosyl)-adenosine N 1-(5-phosphoribosyl)-adenosine 5′-monophosphate N 1-(5-phosphoribosyl)-adenosine 5′-triphosphate N 1-(ribosyl)-adenosine N 1-(ribosyl)-adenosine 5′-monophosphate NAD glycohydrolase NADase Phosphoribosyl-AMP pRib-Ado pRib-AMP pRib-ATP Pyrophosphatase Rib-Ado Rib-AMP |
| Title | Hydrolysis of the phosphoanhydride linkage of cyclic ADP‐ribose by the Mn2+‐dependent ADP‐ribose/CDP‐alcohol pyrophosphatase |
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