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Issue 8, 1999
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Why is the antiviral nucleotide analogue 9-[2-(phosphonomethoxy)ethyl]adenine in its diphosphorylated form (PMEApp4–) initially a better substrate for polymerases than (2′-deoxy)adenosine 5′-triphosphate (dATP4–/ATP4–)? Considerations on the mechanism of nucleic acid polymerases

Abstract

The observation that the antivirally active PMEA in its diphosphorylated form (PMEApp4–) is initially a better substrate for polymerases than dATP4– (ATP4–) can be rationalized by (i) the increased basicity of the phosphonyl group (compared to a phosphoryl group) and (ii) the participation of the ether O atom of PMEApp4– in metal ion binding; both effects together favor M2+ binding at the α group and thus its nucleophilic attack.

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Article information


Chem. Commun., 1999, 743-744
Article type
Paper

Why is the antiviral nucleotide analogue 9-[2-(phosphonomethoxy)ethyl]adenine in its diphosphorylated form (PMEApp4–) initially a better substrate for polymerases than (2′-deoxy)adenosine 5′-triphosphate (dATP4–/ATP4–)? Considerations on the mechanism of nucleic acid polymerases

H. Sigel, B. Song, C. A. Blindauer, L. E. Kapinos, F. Gregáň and N. Prónayová, Chem. Commun., 1999, 743
DOI: 10.1039/A901233H

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