158700-26-6Relevant articles and documents
Synthesis and reactions of nucleoside 5'-diphosphate imidazolide. A nonenzymatic capping agent for 5'-monophosphorylated oligoribonucleotides in aqueous solution
Sawai, Hiroaki,Wakai, Hiromichi,Nakamura-Ozaki, Akiko
, p. 5836 - 5840 (1999)
We have synthesized adenosine and 7-methylguanosine 5'-diphosphate imidazolides from imidazole and the corresponding nucleoside 5'-diphosphates. The phosphorimidazolide bond of the compounds was susceptible to hydrolysis and hydrolyzed gradually in neutral aqueous solution, but it was more stable than that of the corresponding imidazolides of nucleoside 5'-monophosphate. The 7-methylguanosine 5'-diphosphate imidazolide reacted with guanosine 5'- monophosphate or 5' monophosphorylated oligoribonucleotides in neutral aqueous solution in the presence of an Mn2- ion catalyst converting to the cap portion of mRNA or the capped m7Gppp-oligoribonucleotides in substantial yields. The condensation reaction of adenosine 5'-diphosphate imidazolide with adenosine 5'-monophosphate took place similarly in neutral aqueous solution by a divalent metal ion-catalyst such as Mg2+ or Mn2+, yielding diadenosine 5',5'-triphosphate.
Solid-phase synthesis of symmetrical 5′,5′-dinucleoside mono-, di-, tri-, and tetraphosphodiesters
Ahmadibeni, Yousef,Parang, Keykavous
, p. 4483 - 4486 (2008/03/12)
(Chemical Equation Presented) Four classes of phosphitylating reagents were subjected to reactions with aminomethyl polystyrene resin-bound p-acetoxybenzyl alcohol to yield the corresponding polymer-bound mono-, di-, tri-, and tetraphosphitylating reagents. The solid-phase reagents were reacted with unprotected nucleosides (e.g., thymidine, adenosine, 3′-azido-3′- deoxythymidine, cytidine, or inosine) in the presence of 5-(ethylthio)-1H- tetrazole. Polymer-bound nucleosides underwent oxidation with fert-butyl hydroperoxide, deprotection of cyanoethoxy groups with DBU, and the acidic cleavage, respectively, to afford 5′,5′-dinucleoside mono-, di-, tri-, and tetraphosphodiesters in 59-78% yield.
Engineering human FHIT, a diadenosine triphosphate hydrolase, into an efficient dinucleoside polyphosphate synthase
Huang, Kaisheng,Frey, Perry A.
, p. 9548 - 9549 (2007/10/03)
The putative human tumor suppressor gene FHIT encodes Fhit, the fragile histidine triad protein. Fhit is thought to participate in a signal transduction pathway involving dinucleoside polyphosphates. Fhit catalyzes the Mg2+-dependent hydrolysis of P1-5′-O-adenosine-P3-5′-O-adenosine triphosphate (Ap3A) to AMP and MgADP. Mutation of His96 to glycine disables Fhit as a catalyst for the hydrolysis of phosphoanhydrides such as Ap3A. However, the mutated enzyme H96G-Fhit efficiently catalyzes the synthesis of phosphoanhydride bonds in reactions of nucleoside-5′-phosphimidazolides with nucleoside di- and triphosphates. H96G-Fhit can be employed in the synthesis of a wide range of dinucleoside tri- and tetraphosphates. We here describe the use of H96G-Fhit to catalyze the synthesis of Ap3A, Ap3C, Ap3G, Ap3T, Ap3U, Cp3U, Tp3U, dAp3U, Ap4A, Ap4U, and the fluorescent Ap4etheno-C. Copyright
