Target intelligence / Profile preview

DNA polymerase; Ribonucleotide reductase (null; RNR)

Target
null; RNR
Molecular classification
Enzyme, Class I Ribonucleotide reductase, Class II Ribonucleotide reductase, Class III Ribonucleotide reductase
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Overview

DNA polymerase is an enzyme that synthesizes DNA from deoxyribonucleotide triphosphates, using a template strand to ensure accurate DNA replication and repair. Therapeutic targeting exploits its crucial role in replication and repair, notably in cancer and viral infections. Ribonucleotide reductase is the rate-limiting enzyme responsible for the conversion of ribonucleotides to deoxyribonucleotides, the essential substrates for DNA synthesis and repair; its activity is tightly regulated and integral for maintaining balanced dNTP pools. Both enzymes are critical for cell proliferation, and their inhibition forms the basis for multiple classes of anti-cancer and antiviral drugs.

Other names
DNA-dependent polymerasepolribonucleoside diphosphate reductase
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Mechanism of action

Inhibitors of DNA polymerase act primarily as nucleoside/nucleotide analogs causing chain termination or inhibiting DNA synthesis; some are DNA damaging agents; others target specific polymerases (replication vs repair). RNR inhibitors include substrate analogs (e.g., gemcitabine), free radical scavengers (e.g., hydroxyurea), and compounds that inhibit subunit interaction or cofactor activity.

03

Biological functions

DNA replicationDNA repairtranslesion synthesisDe novo synthesis of deoxyribonucleotidesregulation of dNTP pools
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Disease associations

Cancerviral infectionbacterial infectionautoimmune disordersproliferative disorders
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Safety considerations

Myelosuppressiontoxicity due to off-target effects on mitochondrial/repair polymerasesresistancemutagenesiscytopenias
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Interacting drugs

Acyclovir

11 more in the full profile.

07

Biomarkers

Proliferative index (e.g., S-phase fraction)expression levelsmutational status

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