92587-94-5

Upstream product

• 1032-65-1 cytidine 5'-(dihydrogen phosphate) 
• 800-73-7 dCDP 
• 951-77-9 2'-Deoxycytidine 
• 1233921-79-3 C₉H₁₂Cl₂N₃O₅P 

Downstream Products

• 31747-59-8 5-iodo-2′-deoxycytidine triphosphate 
• 951-77-9 2'-Deoxycytidine 
• 110537-14-9 N4-(6-aminohexyl)-dCTP 
• 800-73-7 dCDP 

Relevant academic research and scientific papers

An improved protection-free one-pot chemical synthesis of 2′-deoxynucleoside-5′-triphosphates

□ A facile, straightforward, reliable, and an efficient method for the gram-scale chemical synthesis of both purine deoxynucleotides such as 2 ′-deoxyguanosine-5 ′-triphosphate (dGTP) and 2 ′- deoxyadenosine-5′-triphosphate (dATP) and pyrimidine deoxynucleotides such as 2 ′-deoxycytidine- 5 ′-triphosphate (dCTP), thymidine-5 ′-triphosphate (TTP), and 2 ′-deoxyuridine-5 ′-triphosphate (dUTP) starting from the corresponding nucleoside is described. This improved "one-pot, three step"Ludwig synthetic strategy involves the monophosphorylation of nucleoside followed by reaction with tributylammonium pyrophosphate and hydrolysis of the resulting cyclic intermediate to provide the corresponding dNTP in good yields (65%-70%). Copyright Taylor and Francis Group, LLC.

P(V) Reagents for the Scalable Synthesis of Natural and Modified Nucleoside Triphosphates

Natural and modified nucleoside triphosphates impact nearly every major aspect of healthcare research from DNA sequencing to drug discovery. However, a scalable synthetic route to these molecules has long been hindered by the need for purification by high performance liquid chromatography (HPLC). Here, we describe a fundamentally different approach that uses a novel P(V) pyrene pyrophosphate reagent to generate derivatives that are purified by silica gel chromatography and converted to the desired compounds on scales vastly exceeding those achievable by HPLC. The power of this approach is demonstrated through the synthesis of a broad range of natural and unnatural nucleoside triphosphates (dNTPs and xNTPs) using protocols that are efficient, inexpensive, and operationally straightforward.

COMPOSITIONS AND METHODS FOR SYNTHESIS OF PHOSPHORYLATED MOLECULES

The invention provides compositions and methods for synthesis of phosphorylated organic compounds, including nucleoside triphosphates.

Synthetic method of nucleoside tetraphosphate

The invention discloses a synthetic method of nucleoside tetraphosphate. The synthetic method comprises the steps of carrying out selective phosphorylation reaction by virtue of nucleoside and a cyclic phosphorylation reagent, and carrying out oxidation and hydrolysis loop opening, so as to obtain nucleoside tetraphosphate. The structure of the cyclic phosphorylation reagent is represented by a formula I (shown in the description). According to the synthetic method, 5'-nucleoside tetraphosphate is selectively generated from nucleoside under the effect of the high-selectivity phosphorylation reagent, and 3'-OH (and 2'-OH) does not need to be protected in the process, namely that the generaiton of 3'(and 2'-)tetraphosphate can be effectively inhibited. Nucleoside tetraphosphate synthesized by virtue of the method has wide use ranges in the biology fields of DNA sequencing, labeling, extension and the like; currently, the selling prices is expensive, a synthetic method is complex, the reaction selectivity is poor; and the synthetic method provided by the invention is good in selectivity and easy in separation and purification, required experimental conditions are simple, and the synthetic processes are all conventional chemical reactions, so that the synthetic method is applicable to large-scale popularization and use.

Substrate specificity of T5 bacteriophage deoxyribonucleoside monophosphate kinase and its application for the synthesis of [α-32P]d/rNTP

Bacteriophage T5 deoxynucleoside monophosphate kinase (dNMP kinase, EC 2.7.4.13) is shown to catalyze the phosphorylation of both d2CMP and ribonucleotides AMP, GMP, and CMP, but does not phosphorylate UMP. For natural acceptors of the phosphoryl group, k m and k cat were found. The applicability of T5 dNMP kinase as a universal enzyme capable of the phosphorylation of labelled r/dNMP was shown for the synthesis of [α- 32P]rNTP and [α-32P]dNTP.

A novel method for the preparation of nucleoside triphosphates from activated nucleoside phosphoramidates

A novel method for the preparation of nucleoside triphosphates has been developed. The strategy employs a highly reactive pyrrolidinium phosphoramidate zwitterion intermediate that undergoes efficient coupling with tris(tetra-n-butylammonium) hydrogen pyrophosphate to generate nucleoside triphosphate.

Identification of enzymes catalyzing two-step phosphorylation of cidofovir and the effect of cytomegalovirus infection on their activities in host cells

Cidofovir [CDV; (S)-1-(3-hydroxy-2-phosphonomethoxyethyl)-cytosine] is an acyclic nucleotide analog with potent and selective in vitro and in vivo activities against a broad spectrum of herpesviruses and other DNA viruses. We studied the mechanism of enzymatic synthesis of CDV diphosphate, the putative antiviral metabolite of CDV. The phosphorylation is two-step process catalyzed by several enzymes. An enzymatic activity phosphorylating CDV to its monophosphate derivative was purified from human liver and identified as pyrimidine nucleoside monophosphate kinase (EC 2.7.4.14.). CDV (K(m) = 2.10 ± 0.18 mM and V(max) = 1.10 ± 0.05 μmol/min/mg) was found to be a substantially weaker substrate for purified enzyme than CMP, UMP, or dCMP. Pyrimidine nucleoside monophosphate kinase was used for preparative enzymatic synthesis of CDV monophosphate. Pyruvate kinase (EC 2.7.1.40), creatine kinase (EC 2.7.3.2), and nucleoside diphosphate kinase (EC 2.7.4.6) were found to catalyze CDV diphosphate synthesis from CDV monophosphate, whereas phosphoglycerate kinase (EC 2.7.2.3) and succinyl-CoA synthetase (EC 6.2.1.4) did not. Based on V(max)/K(m) (phosphorylation efficiency) values determined with enzymes purified from human sources, the most efficient phosphorylation of CDV monophosphate is catalyzed by pyruvate kinase. After infection of human lung fibroblasts with cytomegalovirus, the intracellular activities of pyrimidine nucleoside monophosphate kinase, pyruvate kinase, creatine kinase, and nucleoside diphosphate kinase increased 2-, 1.3-, 3-, and 5-fold, respectively. The metabolism of [3H]CDV in mock- and cytomegalovirus-infected cells was examined. The intracellular levels of CDV monophosphate and CDV diphosphate increased ~20- and 8-fold, respectively, in cytomegalovirus-infected cells, presumably due to the stimulation of CDV uptake and higher activities of phosphorylating enzymes.