title: Position of cyclization in cyclic ADP-ribose.
abstract: Cyclic adenosine diphosphoribose (cADPR) is a putative second messenger of calcium homeostasis synthesized from NAD by cleavage of the nicotinamide-ribose bond and cyclization of the ribose to the adenine ring. In this study, the ultraviolet absorption spectra of cADPR have been studied as a function of pH and compared to other compounds containing an adenine ring with substitutions at known positions. The results support a structure for cADPR in which cyclization is to position 1 of the adenine ring, rather than to N6, as has been previously proposed.
authors.affiliation: Division of Medicinal Chemistry & Pharmaceutics, College of Pharmacy, University of Kentucky, Lexington 40536.
authors.forename: H
authors.initials: H
authors.lastname: Kim
authors.forename: E L
authors.initials: EL
authors.lastname: Jacobson
authors.forename: M K
authors.initials: MK
authors.lastname: Jacobson
mesh_terms: D000225:Adenine / Q000031:analogs & derivatives; D000241:Adenosine / Q000031:analogs & derivatives; D000246:Adenosine Diphosphate Ribose / Q000031:analogs & derivatives* / Q000737:chemistry; D036563:Cyclic ADP-Ribose; D006863:Hydrogen-Ion Concentration; D008956:Models, Chemical; D013056:Spectrophotometry, Ultraviolet
chemical_list: D036563:Cyclic ADP-Ribose; D000246:Adenosine Diphosphate Ribose; D000225:Adenine; D000241:Adenosine