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DNA and RNA polymerases, along with related nucleotide-processing enzymes (including nucleases), are a superfamily of enzymes essential for nucleic acid metabolism. DNA polymerases catalyze the synthesis of DNA from deoxynucleoside triphosphates using a DNA template, playing critical roles in DNA replication and repair. RNA polymerases catalyze the transcription of DNA to synthesize RNA, regulating gene expression and enabling cellular function. Nucleotide-processing enzymes such as nucleases cleave nucleic acids for repair, recombination, or degradation. These targets are highly conserved, essential for cell survival, and key regulators of biological information flow. They are prominent therapeutic targets for antiviral, anticancer, and antimicrobial agents due to their indispensable roles in cell division and viral replication. Targeting these enzymes, however, can present significant safety and selectivity challenges, since inhibition in host tissues can disrupt normal cell function and lead to toxicity.
Competitive inhibition by nucleoside/nucleotide analogs, which are incorporated in place of natural nucleotides and terminate chain elongation or introduce mutations; Allosteric inhibition of enzyme active site; Inhibition of binding to DNA or template RNA; Interference with enzyme-substrate recognition
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