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

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Structured PICO

Population

Nucleic acid polymerases

Intervention

9-[2-(phosphonomethoxy)ethyl]adenine in its diphosphorylated form (PMEApp4-)

Comparator

(2'-deoxy)adenosine 5'-triphosphate (dATP4-/ATP4-)

Outcome

Substrate preference and mechanism of metal ion binding

The study provides a biochemical rationale for why the antiviral nucleotide analogue PMEA is a preferred substrate for polymerases.

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Biochemical rationale for PMEA polymerase preference is preliminary; leaves open translation to antiviral efficacy or clinical use.

Sigel et al. (1999) studied this question.

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