| 词条 | Cyclic ADP-ribose |
| 释义 |
| Verifiedfields = changed | Watchedfields = changed | verifiedrevid = 424586166 | ImageFile = Cyclic ADP ribose.svg | ImageSize = 175px | IUPACName = | OtherNames = |Section1={{Chembox Identifiers | CASNo_Ref = {{cascite|correct|??}} | CASNo = 119340-53-3 | PubChem = 123847 | ChEBI_Ref = {{ebicite|changed|EBI}} | ChEBI = 31445 | IUPHAR_ligand = 2445 | MeSHName = Cyclic+ADP-Ribose | ChemSpiderID_Ref = {{chemspidercite|changed|chemspider}} | ChemSpiderID = 21403087 | SMILES = O[C@H]5[C@@H](O)[C@H]2O[C@@H]5COP(O)(=O)OP(O)(=O)OC[C@H]4O[C@@H](N3\\C=N/c1c(ncn12)C3=N)[C@H](O)[C@@H]4O | 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 | StdInChI_Ref = {{stdinchicite|changed|chemspider}} | StdInChI = 1S/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 | StdInChIKey_Ref = {{stdinchicite|changed|chemspider}} | StdInChIKey = BQOHYSXSASDCEA-KEOHHSTQSA-N |Section2={{Chembox Properties | Formula = C15H21N5O13P2 | MolarMass = 541.301 | Appearance = | Density = | MeltingPt = | BoilingPt = |Section3={{Chembox Hazards | MainHazards = | FlashPt = | AutoignitionPt = }} Cyclic ADP Ribose, frequently abbreviated as cADPR, is a cyclic adenine nucleotide (like cAMP) with two phosphate groups present on 5' OH of the adenosine (like ADP), further connected to another ribose at the 5' position, which, in turn, closes the cycle by glycosidic bonding to the nitrogen 1 (N1) of the same adenine base (whose position N9 has the glycosidic bond to the other ribose).[1][2] The N1-glycosidic bond to adenine is what distinguishes cADPR from ADP-ribose (ADPR), the non-cyclic analog. cADPR is produced from nicotinamide adenine dinucleotide (NAD+) by ADP-ribosyl cyclases (EC 3.2.2.5) as part of a second messenger system. FunctioncADPR is a cellular messenger for calcium signaling.[3] It stimulates calcium-induced calcium release at lower cytosolic concentrations of Ca2+. Primary target of cADPR is the ER Ca2+ uptake mechanism. Potentiation of Ca2+ release by cADPR is mediated by increased accumulation of Ca2+ in the SR.[4] MetabolismcADPR and ADPR are synthesized from NAD+ by the bifunctional ectoenzymes of the CD38 family (also includes the GPI-anchored CD157 and the specific, monofunctional ADP ribosyl cyclase of the mollusc Aplysia).[5][6][7] The same enzymes are also capable of hydrolyzing cADPR to ADPR. Catalysis proceeds via a covalently bound intermediate. The hydrolysis reaction is inhibited by ATP, and cADPR may accumulate. Synthesis and degradation of cADPR by enzymes of the CD38 family involve, respectively, the formation and the hydrolysis of the N1-glycosidic bond. In 2009, the first enzyme able to hydrolyze the phosphoanhydride linkage of cADPR, i.e. the one between the two phosphate groups, has been reported.[8] See also
References1. ^{{cite journal |vauthors=Lee HC, Walseth TF, Bratt GT, Hayes RN, Clapper DL |title=Structural determination of a cyclic metabolite of NAD+ with intracellular Ca2+-mobilizing activity |journal=J. Biol. Chem. |volume=264 |issue=3 |pages=1608–15 |year=1989 |pmid=2912976}} 2. ^{{cite journal |vauthors=Lee HC, Aarhus R, Levitt D |title=The crystal structure of cyclic ADP-ribose |journal=Nat. Struct. Biol. |volume=1 |issue=3 |pages=143–4 |year=1994 |pmid=7656029 |doi=10.1038/nsb0394-143}} 3. ^{{cite journal |author=Guse AH |title=Regulation of calcium signaling by the second messenger cyclic adenosine diphosphoribose (cADPR) |journal=Curr. Mol. Med. |volume=4 |issue=3 |pages=239–48 |year=2004 |pmid=15101682 |doi=10.2174/1566524043360771}} 4. ^{{Cite journal|pages=614–22|pmid=11577027|doi=10.1161/hh1901.098066|year=2001|author1=Lukyanenko|first1=V|title=Potentiation of Ca(2+) release by cADP-ribose in the heart is mediated by enhanced SR Ca(2+) uptake into the sarcoplasmic reticulum|journal=Circulation Research|volume=89|issue=7|last2=Györke|first2=I|last3=Wiesner|first3=T. F.|last4=Györke|first4=S}} 5. ^{{cite journal |vauthors=Prasad GS, McRee DE, Stura EA, Levitt DG, Lee HC, Stout CD |title=Crystal structure of Aplysia ADP-ribosyl cyclase, a homolog of the bifunctional ectozyme CD38 |journal=Nat. Struct. Biol. |volume=3 |issue=11 |pages=957–64 |year=1996 |pmid=8901875 |doi=10.1038/nsb1196-957}} 6. ^{{cite journal |vauthors=Liu Q, Kriksunov IA, Graeff R, Munshi C, Lee HC, Hao Q |title=Crystal structure of the human CD38 extracellular domain |journal=Structure |volume=13 |issue=9 |pages=1331–9 |year=2005 |pmid=16154090 |doi=10.1016/j.str.2005.05.012}} 7. ^{{cite journal |author=Guse AH |title=Biochemistry, biology, and pharmacology of cyclic adenosine diphosphoribose (cADPR) |journal=Curr. Med. Chem. |volume=11 |issue=7 |pages=847–55 |year=2004 |pmid=15078169 |doi=10.2174/0929867043455602}} 8. ^{{cite journal |vauthors=Canales J, Fernández A, Rodrigues JR, Ferreira R, Ribeiro JM, Cabezas A, Costas MJ, Cameselle JC |title=Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase |journal=FEBS Lett. |volume=583 |year=2009 |issue=10 |pages=1593–8 |pmid=19379742 |doi=10.1016/j.febslet.2009.04.023}} External links
2 : Nucleotides|Cyclic nucleotides |
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