DNA polymerase

DNA polymerase is an enzyme essential for the synthesis of DNA molecules from deoxynucleoside triphosphates, playing a central role in DNA replication and repair in all living cells[1][5][6]. Inhibitors of DNA polymerase block DNA strand elongation or incorporation, interfering with DNA replication and cell division; this mechanism underlies the action of several anticancer and antiviral drugs[6]. DNA polymerases exist in multiple families (A, B, C, D, X, Y, RT) with specialized functions, structures likened to a right hand with palm, fingers, and thumb subdomains, and typically require divalent metal ions for catalytic activity[2][5][6][8]. Because inhibition of DNA polymerases halts cell proliferation, these enzymes are important therapeutic targets but also pose a risk for toxicity in normal, rapidly dividing cells[6]. Additional details: - "DNA polymerase-mediated DNA synthesis inhibition" is not a canonical target name; the correct target is the enzyme "DNA polymerase". - Multiple small molecule and nucleoside analog drugs inhibit DNA polymerase directly or via incorporation as chain terminators, which is a key therapeutic principle in oncology and antiviral therapy[6]. - Different classes of DNA polymerase exist, including those primarily involved in replication (e.g., polymerase α, δ, ε in eukaryotes) or repair (e.g., polymerase β, λ, μ)[6][8]. - Significant safety concerns arise from inhibition of host DNA polymerases in non-target tissues, particularly in bone marrow, gastrointestinal tract, and in mitochondrial DNA replication (mitochondrial toxicity)[6].

Other names

PolymeraseDeoxyribonucleic acid polymerase

Polymerase inhibition, Chain termination, Competitive inhibition of nucleotide incorporation