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

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• 作者：José ; Canales ; Ascensió ; n Ferná ; ndez ; Joaquim Rui Rodrigues ; Rui Ferreira ; Joã ; o Meireles Ribeiro ; Alicia Cabezas ; Marí ; a Jesú ; s Costas ; José ; Carlos Cameselle
• 关键词：Cyclic ADP-ribose ; ADP-ribose ; Pyrophosphatase ; Phosphoribosyl-AMP ; Histidine biosynthesis ; Immune signaling
• 刊名：FEBS Letters
• 出版年：2009
• 出版时间：19 May 2009
• 年：2009
• 卷：583
• 期：10
• 页码：1593-1598
• 全文大小：453 K

文摘

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.