环ADP核糖

环ADP核糖
识别
CAS号	119340-53-3
PubChem	123847
ChemSpider	21403087
InChI	1/C15H21N5O13P2/c16-12-7-13-18-4-19(12)14-10(23)8(21)5(31-14)1-29-34(25,26)33-35(27,28)30-2-6-9(22)11(24)15(32-6)20(13)3-17-7/h3-6,8-11,14-16,21-24H,1-2H2,(H,25,26)(H,27,28)/t5-,6-,8-,9-,10-,11-,14-,15-/m1/s1;
InChIKey	BQOHYSXSASDCEA-KEOHHSTQBN
ChEBI	31445
MeSH	Cyclic+ADP-Ribose
IUPHAR配体	2445
性质
化学式	C15H21N5O13P2
摩尔质量	541.301 g·mol⁻¹
	若非注明，所有数据均出自标准状态（25 ℃，100 kPa）下。

环ADP核糖（Cyclic ADP Ribose；cADPR）是一种环状腺嘌呤核苷酸，含有两个磷酸基团、两个核糖，以及一个腺嘌呤碱基，是一种钙信号（calcium signaling）的第二信使。

功能

cADPR可作为传递钙信号的细胞内信使^[1]。它是雷诺丁受体的别构调节分子，在低浓度下促进钙的释放。高浓度的咖啡因能活化雷诺丁受体，这被认为是由于咖啡因作为cADPR的作用。目前还不清楚这种影响是否是由于cADPR直接与雷诺丁受体结合，还是间接透过与FKBP12.6结合。

代谢

cADPR和ADPR由CD38家族的双功能外酶从NAD⁺合成（也包括GPI锚定的CD157和软体动物海兔的特定单功能ADP核糖环化酶）。^[2]^[3]^[4]相同的酶也能够将cADPR水解为ADPR。催化作用透过共价结合中间体进行。水解反应被ATP抑制，cADPR可能会聚集。 CD38家族酶对cADPR的合成和降解分别涉及 N1-糖苷键的形成和水解。 2009年，报告了第一个能够水解cADPR的磷酸酐键（即两个磷酸基团之间的键）的酶。^[5]

SARM1和其他含有TIR结构域的蛋白质也催化NAD⁺形成cADPR。^[6]^[7]

参见

参考文献

^ Guse AH. Regulation of calcium signaling by the second messenger cyclic adenosine diphosphoribose (cADPR). Curr. Mol. Med. 2004, 4 (3): 239–48. PMID 15101682.
^ Prasad GS, McRee DE, Stura EA, Levitt DG, Lee HC, Stout CD. Crystal structure of Aplysia ADP-ribosyl cyclase, a homolog of the bifunctional ectozyme CD38. Nat. Struct. Biol. 1996, 3 (11): 957–64. PMID 8901875. S2CID 21978229. doi:10.1038/nsb1196-957.
^ Liu Q, Kriksunov IA, Graeff R, Munshi C, Lee HC, Hao Q. Crystal structure of the human CD38 extracellular domain. Structure. 2005, 13 (9): 1331–9. PMID 16154090. doi:10.1016/j.str.2005.05.012 .
^ Guse AH. Biochemistry, biology, and pharmacology of cyclic adenosine diphosphoribose (cADPR). Curr. Med. Chem. 2004, 11 (7): 847–55. PMID 15078169. doi:10.2174/0929867043455602.
^ Canales J, Fernández A, Rodrigues JR, Ferreira R, Ribeiro JM, Cabezas A, Costas MJ, Cameselle JC. Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn²⁺-dependent ADP-ribose/CDP-alcohol pyrophosphatase. FEBS Lett. 2009, 583 (10): 1593–8. PMID 19379742. S2CID 28571921. doi:10.1016/j.febslet.2009.04.023. hdl:10400.8/3028 .
^ Lee HC, Zhao YJ. Resolving the topological enigma in Ca 2+ signaling by cyclic ADP-ribose and NAADP. Journal of Biological Chemistry. 2019, 294 (52): 19831–19843. PMC 6937575 . PMID 31672920. doi:10.1074/jbc.REV119.009635 .
^ Essuman, Kow; Summers, Daniel W.; Sasaki, Yo; Mao, Xianrong; Yim, Aldrin Kay Yuen; DiAntonio, Aaron; Milbrandt, Jeffrey. TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes. Current Biology. 2018-02-05, 28 (3): 421–430.e4. ISSN 1879-0445. PMC 5802418 . PMID 29395922. doi:10.1016/j.cub.2017.12.024.

外部链接

http://www.tc.umn.edu/~leehc/ （页面存档备份，存于互联网档案馆）

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[1] Guse AH. Regulation of calcium signaling by the second messenger cyclic adenosine diphosphoribose (cADPR). Curr. Mol. Med. 2004, 4 (3): 239–48. PMID 15101682.

[2] Prasad GS, McRee DE, Stura EA, Levitt DG, Lee HC, Stout CD. Crystal structure of Aplysia ADP-ribosyl cyclase, a homolog of the bifunctional ectozyme CD38. Nat. Struct. Biol. 1996, 3 (11): 957–64. PMID 8901875. S2CID 21978229. doi:10.1038/nsb1196-957.

[3] Liu Q, Kriksunov IA, Graeff R, Munshi C, Lee HC, Hao Q. Crystal structure of the human CD38 extracellular domain. Structure. 2005, 13 (9): 1331–9. PMID 16154090. doi:10.1016/j.str.2005.05.012 .

[4] Guse AH. Biochemistry, biology, and pharmacology of cyclic adenosine diphosphoribose (cADPR). Curr. Med. Chem. 2004, 11 (7): 847–55. PMID 15078169. doi:10.2174/0929867043455602.

[5] Canales J, Fernández A, Rodrigues JR, Ferreira R, Ribeiro JM, Cabezas A, Costas MJ, Cameselle JC. Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn²⁺-dependent ADP-ribose/CDP-alcohol pyrophosphatase. FEBS Lett. 2009, 583 (10): 1593–8. PMID 19379742. S2CID 28571921. doi:10.1016/j.febslet.2009.04.023. hdl:10400.8/3028 .

[pmid31672920-6] Lee HC, Zhao YJ. Resolving the topological enigma in Ca 2+ signaling by cyclic ADP-ribose and NAADP. Journal of Biological Chemistry. 2019, 294 (52): 19831–19843. PMC 6937575 . PMID 31672920. doi:10.1074/jbc.REV119.009635 .

[:0-7] Essuman, Kow; Summers, Daniel W.; Sasaki, Yo; Mao, Xianrong; Yim, Aldrin Kay Yuen; DiAntonio, Aaron; Milbrandt, Jeffrey. TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes. Current Biology. 2018-02-05, 28 (3): 421–430.e4. ISSN 1879-0445. PMC 5802418 . PMID 29395922. doi:10.1016/j.cub.2017.12.024.

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