23600-16-0

Upstream product

• 58-64-0 adenosine 5'-diphosphate 
• 23567-97-7 8-bromo-adenosine-5'-triphosphate 

Downstream Products

• 193698-75-8 C₂₇H₄₂N₉O₁₇P₃ 

Relevant academic research and scientific papers

Synthesis and biological activity of a bivalent nucleotide inhibitor of ribonucleotide reductase

A novel nucleotide inhibitor (ADP-S-HBES-S-dGTP) of mouse ribonucleotide reductase was designed to span the active site and the allosteric specificity site of the enzyme. The inhibitor contains ADP and dGTP moieties which are linked by 1,6-hexane-(bis-ethylenesulfone), and has a K(i) value of 12 μM. (C) 2000 Elsevier Science Ltd.

8-(6-Aminohexyl) amino-cyclic ATPR: A new affinity probe for the study of cyclic ADPR-binding proteins

8-(6-Aminohexyl) amino-cyclic ATPR, a new affinity probe for the study of cADPR-binding proteins, was prepared in four steps with an overall yield of 21%.

Hydrolysis of P2-purinoceptor agonists by a purified ectonucleotidase from the bovine aorta, the ATP-diphosphohydrolase.

Pharmacologists are becoming more and more aware of the possibility that certain ATP analogues currently used to classify the P2-purinoceptors are dephosphorylated by ectonucleotidases. In this study, we provide evidence that in the vascular system, these purine analogues are hydrolysed by an ATP-diphosphohydrolase (ATPDase). This enzyme is known as the major plasma membrane nucleotidase of endothelial and smooth muscle cells, and is believed to dephosphorylate extracellular triphospho- and diphosphonucleosides. Assays were conducted with a purified ATPDase from smooth muscle cells of bovine aorta. At a concentration of 250 microM, adenosine 5'-(alpha,beta-methylene) triphosphonate (alpha,beta-metATP), adenosine 5'-(beta,gamma-methylene) triphosphonate (beta,gamma-metATP), adenosine 5'-(alpha,beta-methylene) disphosphonate (alpha,beta-metADP), adenylyl 5'-(beta,gamma-imido) diphosphonate (beta,gamma-imidoATP) and adenosine 5'-O-(2-thiodiphosphate) (ADP beta S) all resisted dephosphorylation, whereas 2-chloroadenosine triphosphate (2-chloroATP), 2-methylthioadenosine triphosphate (2-MeSATP) and 8-bromoadenosine triphosphate (8-bromo-ATP) were hydrolysed at 99, 63, and 20% of the rate of ATP hydrolysis, respectively. All the non-hydrolysable analogues tested, except alpha,beta-metADP, competed with ATP and ADP for the ATPDase catalytic site, reducing their hydrolysis by 35-50%. Apparent Km values for ATP and ADP were estimated at 14.1 and 12.0 microM, respectively, whereas apparent Km and Ki values for the purine analogues ranged from 12 to 28 microM. These results strongly support the view that (1) the ATPDase is expected to reduce substantially the P2-response induced by ATP, ADP, and some hydrolysable agonists; and (2) by competing with the hydrolysis of endogenously released ATP and ADP, non-hydrolysable analogues could alter the amplitude or direction of the cellular response induced by these natural substrates.