Uracil-DNA glycosylase (UDG (also commonly referred to as UNG for "uracil-N-glycosylase"))

Uracil-DNA glycosylase is an evolutionarily conserved enzyme that plays a critical role in genome maintenance by catalyzing the hydrolysis of the N-glycosidic bond between uracil and deoxyribose in DNA. Uracil in DNA arises from either deamination of cytosine or misincorporation during DNA synthesis. UDG detects uracil in both single- and double-stranded DNA, flips the uracil base out of the DNA helix, and excises it, leaving an abasic (apyrimidinic) site. This lesion is subsequently processed by other enzymes in the base excision repair pathway. UDG helps prevent mutagenesis by eliminating erroneous uracil, thus protecting genome integrity. It exists as multiple isoforms in eukaryotes, with UNG1 and UNG2 being the mitochondrial and nuclear forms, respectively. UDG belongs to a superfamily classified into six families based on substrate specificity, and is widely utilized in molecular biology (e.g., PCR contamination control) and studied in the context of cancer therapy, infection, and aging.

Other names

UNG (uracil-N-glycosylase, canonical gene/protein name for the human form)UDGUracil-DNA glycosidase

Enzyme inhibition (small molecules or proteins may inhibit UDG activity); Substrate masking (artificial oligonucleotides or modified uracils shield UDG targets); Sensitization to DNA-damaging agents (UDG inhibition increases cytotoxic impact of uracil incorporation)