Bioorg Med Chem 2004 Jan 15;122:475-87. doi: 10.1016/j.bmc.2003.10.012.

Aplysia californica mediated cyclisation of novel 3''-modified NAD+ analogues: a role for hydrogen bonding in the recognition of cyclic adenosine 5''-diphosphate ribose.

???displayArticle.abstract???
Cyclic ADP-ribose mobilizes intracellular Ca2+ in a variety of cells. To elucidate the nature of the interaction between the C3'' substituent of cADP-ribose and the cADPR receptor, three analogues of NAD+ modified in the adenosine ribase (xyloNAD+ 3''F-xyloNAD+ and 3''F-NAD+ were chemically synthesised from D-xylose and adenine starting materials. 3''F-NAD+ was readily converted to cyclic 3''F-ADP ribose by the action of the cyclase enzyme derived from the mollusc Aplysia californica. XyloNAD+ and 3''F-xyloNAD+ were cyclised only reluctantly and in poor yield to afford unstable cyclic products. Biological evaluation of cyclic 3''F-ADP ribose for calcium release in sea urchin egg homogenate gave an EC(50) of 1.5+/-0.5 microM. This high value suggests that the ability of the C3'' substituent to donate a hydrogen bond is crucial for agonism.

???displayArticle.pubmedLink??? 14723966
???displayArticle.link??? Bioorg Med Chem


Genes referenced: LOC100887844